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Patent 2373850 Summary

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(12) Patent: (11) CA 2373850
(54) English Title: INGESTIBLE AND DEGRADABLE CHEWING GUM INCLUDING ENZYMATIC HYDROLYSATES OF PROTEINS
(54) French Title: GOMME A MACHER INGERABLE ET DEGRADABLE RENFERMANT DES HYDROLYSATS ENZYMATIQUES DE PROTEINES
Status: Expired and beyond the Period of Reversal
Bibliographic Data
(51) International Patent Classification (IPC):
  • A23G 04/00 (2006.01)
  • A23J 03/34 (2006.01)
(72) Inventors :
  • LIU, JINGPING (United States of America)
  • LI, WEISHENG (United States of America)
  • FOSTER, JACK D. (United States of America)
(73) Owners :
  • WM. WRIGLEY JR. COMPANY
(71) Applicants :
  • WM. WRIGLEY JR. COMPANY (United States of America)
(74) Agent: CASSAN MACLEAN
(74) Associate agent:
(45) Issued: 2005-05-24
(86) PCT Filing Date: 2000-03-24
(87) Open to Public Inspection: 2001-01-11
Examination requested: 2001-12-21
Availability of licence: N/A
Dedicated to the Public: N/A
(25) Language of filing: English

Patent Cooperation Treaty (PCT): Yes
(86) PCT Filing Number: PCT/US2000/007809
(87) International Publication Number: US2000007809
(85) National Entry: 2001-12-21

(30) Application Priority Data:
Application No. Country/Territory Date
60/141,603 (United States of America) 1999-06-30

Abstracts

English Abstract


Ingestible and degradable gum bases and chewing gums including enzymatically
hydrolyzed zero are provided.
Additionally, methods of producing gum bases and chewing gums are provided.


French Abstract

L'invention concerne des bases pour gomme à mâcher et des gommes à mâcher ingérables et dégradables renfermant de la zéine ayant subi une hydrolyse enzymatique. L'invention concerne en outre des procédés relatifs à l'élaboration de bases pour gomme à mâcher et de gommes à mâcher.

Claims

Note: Claims are shown in the official language in which they were submitted.


WE CLAIM:
1. A gum base comprising enzymatically hydrolyzed zein.
2. The gum base of Claim 1 wherein the zein is hydrolyzed with a peptidase.
3. The gum base of Claim 1 wherein the zein is hydrolyzed with a
proteinase.
4. The gum base of Claim 1 including a humectant.
5. The gum base of Claim 1 including an emulsifier.
6. The gum base of Claim 1 including a polysaccharide.
7. The gum base of Claim 1 including an ingestible protein.
8. The gum base of Claim 1 including a lipid.
9. The gum base of Claim 1 wherein the enzymatically hydrolyzed zero
comprises approximately 20% to about 65% percent by weight of the gum base.
10. The gum base of Claim 1 including an edible acid.
11. The gum base of Claim 1 wherein the zein is derived from corn.
12. A chewing gum base comprising enzymatically hydrolzyed zero and a
polysaccharide.
13. The gum base of Claim 12 including a humectant.
21

14. The gum base of Claim 12 including an emulsifier.
15. The gum base of Claim 12 including an ingestible protein.
16. The gum base of Claim 12 including a lipid.
17. The gum base of Claim 12 wherein the enzymatically hydrolyzed zero
comprises approximately 20% to about 65% percent by weight of the gum base.
18. The gum base of Claim 12 including an edible acid.
19. A chewing gum comprising:
a gum base including enzymatically hydrolyzed zero; and
a flavor and a sweetener.
20. The chewing gum of Claim 19 wherein the zero is hydrolyzed with a
peptidase.
21. The chewing gum of Claim 19 wherein the zero is hydrolyzed with a
proteinase.
22. The chewing gum of Claim 19 including a humectant.
23. The chewing gum of Claim 19 including an emulsifier.
24. The chewing gum of Claim 19 including a polysaccharide.
25. The chewing gum of Claim 19 including a digestible protein.
26. The chewing gum of Claim 19 including a lipid.
27. The chewing gum of Claim 19 wherein the enzymatically hydrolyzed zero
22

comprises approximately 20% to about 65% percent by weight of the gum base.
28. The chewing gum of Claim 19 wherein the zero is derived from corn.
29. The chewing gum of Claim 19 including malt.
30. A method for making gum base comprising the steps of
hydrolyzing zero using an enzyme; and
using the enzymatically hydrolyzed zero to produce a gum base.
31. A method for making chewing gum comprising the steps of:
providing a gum base including an enzymatically hydrolyzed zero; and
mixing the gum base with a flavor and a sweetener to provide a finished
chewing
gum.
32. The method of Claim 31 wherein the finished chewing gum is heated.
23

Description

Note: Descriptions are shown in the official language in which they were submitted.


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SPECIFICATION
TITLE
"INGESTIBLE AND DEGRADABLE CHEWING GUM
INCLUDING ENZYMATIC HYDROLYSATES OF PROTEINS"
BACKGROUND OF THE INVENTION
The present invention relates generally to chewing gum and the manufacture of
same. More specifically, the present invention relates to chewing gum bases
and
methods and materials for manufacturing same.
Of course, it is known in the manufacture of chewing gum to use a gum base
which is water-insoluble, the water-insoluble gum base is combined with water-
soluble
components such as flavors and sweeteners to produce chewing gum. The water
insoluble portion, or gum cud, is designed not to dissolve in the mouth of the
chewer.
This has resulted in conventional gum cuds that cannot be digested by the
chewer.
Accordingly, after chewing gum is chewed, the gum cud that remains that must
be
discarded. This can create a number of issues with respect to chewing gum.
Unfortunately, conventional gum cuds can easily adhere to any dry surface,
such
as wood, concrete, paper and cloth. When gum cuds are improperly discarded,
they can
be difficult to remove from such surfaces. At times, this has caused some
environmental
concerns.
The above factors may at times restrict the marketing and use of chewing gum.
Accordingly, there has been a move to develop a chewing gum which is either
ingestible
or that creates a gum cud that is easily removable and degradable. However,
this search
has been elusive.
For example, typically ingestible polymers, such as proteins and
polysaccharides,
as compared to flexible elastomers that are used in conventional chewing gum,
are rigid
and therefore are not suitable as chewing elastomers. Moreover, in the
presence of large
amounts of plasticizers, such as water, alcohol, and glycerin or polyols, some
proteins
and polysaccharides become elastic at body temperature. On the other hand,
some other
ingestible polymers such as starches, albumins, globulins, due to their polar
structures,
have a tendency to quickly dissolve or disperse in the mouth of the chewer.
Such
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ingestible polymers therefore cannot stand up to prolonged chewing.
Water insoluble ingestible polymers such as prolamines and glutelins have been
explored for formulating ingestible chewing gums. However, the most effective
prolamine solvents such as alcohol and polyol are still water-soluble or
dispersable in
water. They therefore can be extracted out during chewing. The texture of
prolamines,
such as zero, firms up after the alcohol plasticizers have been chewed out.
Accordingly,
water insoluble plasticizers are required in order to maintain a soft texture
during
prolonged chew. This requires the use of lipids such as beeswax, candelilla
wax and fats
to be used for this purpose in the presence of large amounts of emulsifiers.
Chewing gums comprising prolamines as well as zero have been used or
proposed. See, for example, U.S. Patent Nos. 2,154,482, 2,469,861, 2,489,147,
5,482,722 and 5,112,625. However, these products have not been entirely
satisfactory
from a chewing gum standpoint.
There is therefore a need for an improved chewing gum and gum base that is
ingestible and/or biodegradable.
SUMMARY OF THE INVENTION
The present invention provides improved chewing gum and gum bases. The
improved chewing gum and gum bases are ingestible and/or biodegradable.
To this end, the present invention provides a gum base comprising
enzymatically
hydrolyzed zero.
In an embodiment, the zero is hydrolyzed with a peptidase.
In an embodiment, the zero is hydrolyzed with a proteinase.
In an embodiment, the gum base includes a humectant.
In an embodiment, the gum base includes an emulsifier.
In an embodiment, the gum base includes a polysaccharide.
In an embodiment, the gum base includes an ingestible protein.
In an embodiment, the gum base includes a lipid.
In an embodiment, the enzymatically hydrolyzed zero comprises approximately
20% to about 65% percent by weight of the gum base.
In an embodiment, the gum base includes an edible acid.
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In another embodiment of the present invention, a gum base is provided
comprising an enzymatically hydrolyzed protein and a polysaccharide.
In a still further embodiment of the present invention, a chewing gum is
provided.
The chewing gum comprises an insoluble gum base including enzymatically
hydrolyzed
zero and a water soluble portion including a flavor and a sweetener.
In an embodiment, the zero is hydrolyzed with a peptidase.
In an embodiment, the zero is hydrolyzed with a proteinase.
In an embodiment, the chewing gum includes a humectant.
In an embodiment, the chewing gum includes an emulsifier.
In an embodiment, the chewing gum includes a polysaccharide.
In an embodiment, the chewing gum includes an ingestible protein.
In an embodiment, the chewing gum includes a lipid.
In an embodiment, the enzymatically hydrolyzed zero comprises approximately
20% to about 65% percent by weight of the chewing gum base.
In an embodiment, the zero is derived from corn.
In an embodiment, the chewing gum includes malt.
In an further embodiment of the present invention, a method for manufacturing
a chewing gum is provided. The method comprises the steps of hydrolyzing zero
using
an enzyme and using the enzymatically hydrolyzed zero to produce a gum base.
In a still further embodiment of the present invention, a method for
manufacturing
chewing gum is provided. The method comprises the steps of providing a gum
base
including an enzymatically hydrolyzed zero; and mixing with the gum base a
flavor and
a sweetener to provide a finished chewing gum.
In an embodiment of the method, the finished chewing gum is heated.
Accordingly, it is an advantage of the present invention to provide an
improved
chewing gum.
Another advantage of the present invention is to provide an improved gum base.
Still another advantage of the present invention is to provide a gum cud that
is
ingestible. Furthermore, an advantage of the present invention is to provide a
chewing gum that produces a gum cud that does not cause environmental concerns
if
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improperly discarded.
Further an advantage of the present invention is to provide new ingredients
for
constructing gum bases.
Another advantage of the present invention is to provide improved elastomers
for
constructing chewing gum.
Still an advantage of the present invention is to provide an improved method
for
manufacturing chewing gum.
Additional features and advantages of the present invention are described in,
and
will be apparent from, the detailed description of the presently preferred
embodiments
and the figure.
BRIEF DESCRIPTION OF THE FIGURE
Figure 1 illustrates graphically carbon conversation versus biodegradation
over
time (days) for Kraft paper, cellulose, and enzymatic zero gum base.
DETAILED DESCRIPTION OF THE PRESENTLY PREFERRED
EMB ODIMENTS
The present invention provides improved chewing gum, improved gum bases, and
methods of manufacturing same.
Pursuant to the present invention, an enzymatic hydrolysate of protein is used
to
construct chewing gum. Specifically, an enzymatic hydrolsate of zero is used.
This
affords a gum base, or chewing gum, having a number of advantages.
One of the essential requirements for a chewable material is that its glass
transition temperature should not be higher than the temperature of the mouth
of the
chewer. It is well known that water is an important plasticizer for most food
polymers.
Water decreases the glass transition temperature of most biological materials
from about
200°C to about -10°C or so under physiological conditions of
water content.
Without water, most biopolymers would be glassy. For many polysaccharides and
proteins, including zero, gelatin, gluten, starches and maltodextrins, their
dry glass
transition temperatures are in the range of 200°C+/-50°C; at a
water content around 20+/-
5% (wt.), their glass transition temperatures are around room temperature.
Human saliva consists mainly of water and can be a plasticizer for food
polymers
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during chewing. For most hydrophilic food polymers, the water absorbing
capacity is
usually too high or is unlimited. This results in the dissolution or
dispersion of the food
polymers inside the mouth. Therefore, such products can not withstand
prolonged
chewing.
For hydrophobic food polymers such as zero, however, the water holding
capacity
is quite low, which results in a firm texture. Zein is composed of more than
50%
nonpolar amino acid residuals such as leucine, isoleucine, valine, alanine,
proline, and
glutamine. This renders zero primarily soluble in alcoholic solvents and
insoluble in
water.
Chemically intact zero has a moisture absorption capacity of less than 20%. In
order to make a lipid-free ingestible chewing gum with zero one must balance
its water
retention ability and water solubility.
Another important characteristic of chewing gums is the balance of easy
deformation under small force and relatively high cohesive strength to prevent
the gum
from falling apart during chewing. In conventional chewing gums, tackifiers
play an
important role in balancing deformation and cohesion. For the same reason, low
and
medium molecular weight ingredients other than plasticizers are also required
for
ingestible gum.
Pursuant to the present invention, an enzymatic hydrolysate of zero is used to
overcome these two problems. A significant improvement in solubility and
foaming
properties of zero is achieved. Enzymatic modification of zero exposes
ionizable polar
amino acids. These amino acids are capable of binding much more water than the
nonionized polar groups in the intact zero. The water absorption capacity of
zero
hydrolysate can be 10 times higher than that of normal zero. By controlling
the degree
of hydrolysis of zero, a desired water holding ability can be obtained. In
other words,
the enzymatic hydrolysates of the proteins results in a softer texture than
its original form
in a water-rich environment, such as the mouth.
Furthermore, due to the breakdown of the protein chain during the enzymatic
treatment, a certain quantity of low and medium molecular weight protein
fragments are
produced. Due to the similarity of their chemical structure, these low and
medium
molecular weight species are compatible with zero, and behave more like
tackifiers in
5

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conventional gum bases.
Commerciahy available zein has an average molecular weight of around 35,000
Dalton. After modification by proteases, such as papain, a hydrolysate having
a
molecular weight around 3,?00 to about 5,400 Daltons can be produced. A zein
product
containing a certain amount of hydrolysate and water becomes quite chewable.
Usually, a protein backbone is not very reactive chemically. A peptide bond is
hydrolyzed very slowly at neutral pH and room temperature. However, in the
prcsencc
of protease, or at an extreme pH or high temperature, the process can be
greatly
accelerated. Pursuant to the present invention, enzymes including microbial
(fungal or
I0 bacterial) proteases, plant extracted proteases, and their combinations can
be used.
Preferably, the proteases are endopeptidase; most preferably serine proteases
or titio
proteases or their combinations,
In this regard, proteins can be hydrolyzed by different types of proteases.
The
proteases that can catalyze the hydrolysis of protein can be divided into two
categories:
IS peptidase (exopeptidases); and proteinases {endopeptidases). Exopeptidases
catalyze the
hydrolysis of the N-terminal and C-terminal ends of proteins. Endopeptidases
catalyze
the hydrolysis of peptide bonds within the protein chain.
Depending on the functional groups of the active sites (the amino acid
(peptide)
present), they proteases can be subdivided into serine proteinases, thin or
cysteine
20 proteinases, carboxyl or aspartic proteinases and metalloproteinases. Some
proteases
that can be used in the p~seut invention include: the peptidase Validase FP II
(obtained
from Valley Research, Inc.) that contains a very high level of exopeptide; the
proteinases
Alcalase (obtained from Novo Nordisk BioChem North America, lac.); Alkaline
Protease
(a bacterial protease liquid concentrate obtained from a non-genetically
modified strain
25 of Bacillus licheniformis (b60DAPUlg) obtained from Valley Research Inc:;
Yalidase
TSPZ00 (obtained from Valley Research, Inc.), ProtameX (obtained from Novo
Nordisk
BioChem North America, Inc.) and Neutrase '(obtained from Novo Nordisk BioChem
North America, Inc.) that are characterized primarily by their endopeptidase
activities;
Flavourzym~e (obtained from Novo Nordisk BioChem North America, Inc.) contains
bath
30 endopeptidase and exopeptidase. Two of the proteinases mentioned above
(Alcalase,
Alkaline Protease) improve the soflaess of zero hydroisate significantly.
Other
* Trademarks 6

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proteinases showed moderate effect on the texture of zero after the process.
Zein treated
by peptidases showed little improvement on the texture.
Serine proteinases are characterized by the presence of unique serine hydroxyl
groups on the side chain in each enzyme. There are two families of serine
proteases:
S bacterial protease subtilisin; and trypsin family including chymotrypsin,
trypsin, elastase,
thrombin, plasmin, kallikrein and acrosin. Various serine proteases catalyze
the
hydrolysis reaction in very similar manners but, are different in their
preferences for
amino acid side chains at the cleaved peptide bonds and the residuals at the
neighboring
position. All highly purified proteases demonstrated specificity for certain
peptide bonds
and have little or no action on other peptide bonds. Because chymotrypsin
prefers to
cleave the bonds after large hydrophobic residuals, it should be suitable for
the zero
hydrolysis. The subtilisin family has less distinct preferences at the
residual on the
cleaved peptide bond. It was found that the texture of zero treated by a
subtilisin was soft
and chewable. The resultant hydrolysates can be used as a chewing gum
material.
In thiol protease, the cysteine side chain is the active site. Papain, ficin,
bromelain
and actinidin are typical thiol proteases. When trace amount of papain was
mixed with
zero in a humectant for 2.5 hours at 56°C, the partially hydrolyzed
zero became much
softer than one without papain, as shown in Table 1.
Table 1. Modulus* of Zein Hydrolysates
zero without papain zero with 0.2% papain
modulus (g/s) 150 100
*moduli are measured from a punch test by use of a texture analyzer.
In carboxyl proteases, the carboxyl group, usually aspartyl, is the active
site for
catalyzing hydrolysis of proteins. Such proteases include pepsin, gastricsin
and
chymosin. The texture of zero can be modified by pepsin.
Metalloproteases employ bonded metals, such as Zn~ and Ca~ in their active
sites. Carboxypeptidases A and B, thermolysin, angiotensin-converting enzyme,
enkephalinase, collagenase (Zn~ ) are examples of metalloproteases. When
Neutrase,
a metalloproteinase (Zn) produced by a selected strain of Bacillus
amyloliquefaciens, was
used to treat zero, the hydrolsate was firmer than the one treated by
subtilisin or papain.
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Alkaline Protease Concentrate, a bacterial protease liquid obtained from a non
genetically modified strain of Bacillus licheniformis (660DAPU/g) is an
example of a
protease complex. When zero was treated by trace amount of Alkaline Protease
Concentrate at 60°C for 1 hour in aqueous propylene glycol, it produced
a long-lasting
gum-like chewing texture.
The degree of hydrolysis and the structure of the peptides produced,
determines
the properties of a protein hydrolsate. This in turn is dependent on the
nature of the
protein and the specificity of the enzyme used, as well as the hydrolysis
conditions such
as pH and temperature, time and solvents.
Due to the hydrophobic nature of zero, a homogeneous enzymatic hydrolysis of
zero is very difficult to perform under the conditions for water-soluble
proteins. For
example, when the papain-catalyzed hydrolysis of zero was carried out in a
homogeneous
70% ethanol solution, zero was hydrolyzed to a limited extent and the
hydrolysates had
a considerably higher molecular weight compared to the products obtained in a
suspension system. Fortunately, it has also been found that zero hydrolysates
with a
degree of hydrolysis less than 2% contained many components in different
sizes. The
mixtures of polypeptides had substantially increased solubility even with such
a low
degree of hydrolysis.
The enzymatic zero of the present invention can be used as a mastication
material
alone in the presence of water and with other humectants. It can also be
combined with
other ingestible ingredients to make ingestible gum bases having improved
taste and
texture. Other ingestible ingredients include, but are not limited to one or
more of the
following materials: polysaccharides; proteins or their hydrolysates;
ingestible acids;
emulsifiers; and lipids. Polysaccharides include, but are not limited to:
native starches;
modified starches; dextrins; maltodextrin; hydroxypropylinethylcellulose;
dietary fibers;
pectins; alginates; carrageenan; gellan gum; xanthan gum; gum arabic; and guar
gum or
other natural gums. The preferred polysaccharides are maltodextrin and high-
conversion
dextrins. In a preferred embodiment, the chewing gum bases comprise
approximately
5 to about 10% (wt.) polysaccharides. Among digestible proteins, hydrolyzed
collagens
or gelatins can be used.
The addition of fats to the enzymatic zero containing gum bases had little
effect
8

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on the final gum texture when the content of fats was lower than approximately
12%
(wt). Soya oil slightly decreased the hardness, modulus and springiness, and
increased
the adhesive force as compared to partially hydrogenated soy oil. The addition
of fat-
encapsulated acids, such as citric acid and ascorbic acid, slightly decreased
the hardness,
modulus and adhesive force, increased the springiness of the finish gums.
As noted above, gelatins can also be used in the gum base. When used, the
preferred content of gelatin is around 10 to about 20% (wt.) of the base. By
adding other
protein hydrolysates, for example gelatin hydrolsate, hydrocolloids such as
guar flour,
pectin, maltodextrin and acids one can reduce any bitter taste that may be
present in the
enzymatic zero. High molecular weight hydrolyzed gelatin can also decrease the
adhesive force and increase the springiness of the gums. The addition of
starches and
dextrin can increase the sugar-holding capacity of the gum bases.
In an embodiment of the invention an ingestible and chewable gum base is
provided that is derived from the enzymatic hydrolysate of corn proteins. The
corn
proteins comprise mainly zero.
Pursuant to the present invention, a method for preparing ingestible and
chewable
enzymatic hydrolsate of zero is also provided. The method of this invention
can, but not
necessarily, involve the blending of zero, an enzyme and humectant in a batch
mixer.
This can be done at approximately 20°C to about 65°C for
approximately 1 to about 2
hours. In a preferred embodiment, the process is performed at a temperature of
approximately 45 °C to about 60°C. In an embodiment the method
comprises blending
enzymatic zero, polysaccharides, proteins and/or fats with emulsifiers. This
can be done
at approximately 20°C to about 65°C, preferably at approximately
35 °C to about 45°C
for approximately 1 hour.
In a further embodiment of the present invention, sugarless, ingestible
chewing
gums are provided comprising enzymatic hydrolsate of zein, one or more high-
intensity
sweeteners, flavors and in a preferred embodiment, bitterness masking agents.
The high-
intensity sweeteners can include aspartame, alitame, acesulfame, acesulfame
salt,
sucralose, saccharin, cyclamic acid, thaumatin, monellin, glycyrrhizin,
dihydrochalcones
and stevioside; the preferred amount of high-intensity sweeteners is
approximately 0.5
to about 2% in the finished gum. The enzymatic zero gums can comprise
approximately
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0.5 to about 2% (wt.) flavors such as strawberry, spearmint, vanilla, etc. The
preferred
bitterness masking agent is malt with a preferred content of approximately 5
to about
50%(wt.) in the finished gums.
In another embodiment, the ingestible chewing gums comprise one of the gum
bases described above, one or more flavors, preferably one or more bitterness
masking
agents, one or more sugars andlor one or more high-intensity sweeteners.
Sugars can
include monosaccharides, disaccharides and/or oligosaccharides such as
sucrose,
dextrose, maltose, fructose, levulose, galactose and their combinations.
Preferably, a
sugar content of approximately 30 to about 50%(wt.) is provided in the
finished chewing
gum.
At or above 100°C, all the enzymes will lose their activity almost
immediately.
However, when the enzyme deactivation procedure took place right after the
hydrolysis,
crosslinking of the hydrolysates and the loss of humectant due to the high
deactivation
temperature made it difficult to blend the hydrolsate with other gum
ingredients for
further processing. This resulted in crumbly finished gums. In contrast, there
was little
effect on the gum texture when the thermal deactivation of enzymes was carried
out
immediately after the gum was made. In an embodiment of the present invention,
the
finished chewing gum is heated at an elevated temperature for a short period
of time.
The preferred conditions are approximately 90°C to about 110'C for
approximately 3 to
about 20 minutes in a closed system.
Pursuant to the present invention, the humectants that can be used include
aqueous glycols, polyols or alcohols. In a preferred embodiment, aqueous
propylene
glycol is used. The water content in the humectants should be approximately 5
to about
60%, preferably approximately 30 to about 60%, and most preferably,
approximately 40
to about 60% by weight. The higher the water content in the humectants, the
better the
taste of the hydrolysates.
The protein to humectant ratio should be approximately 0.2 to about 3.0,
preferably approximately 0.5 to about 2, and most preferably approximately 1
to about
1.5.
The peptide bonds cleaved during hydrolysis may form sub-units that react with
other proteins or non-proteins. The content of free amino acids or the
residuals with

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amine or carboxyl side chains will increase with an increase of the hydrolysis
degree.
The pH value of the entire system tends to decrease in the absence of a buffer
solution.
The buffer can help to achieve a hydrolysis degree (HD) of the hydrolysates.
Gum-grade
hydrolysate can be prepared with or without buffer.
Table 2 (below) illustrates hydrolysis time versus the degree of hydrolysis.
After
a one-hour hydrolysis, zero became soft and chewable with HD around 1.8%.
Table 2. Hydrolysis time vs. hydrolysis degree
time (min.) 30 60
pH (1%wt solution)5.48 5.41
hydrolysis degree0.8 1.8
%
Table 3 (below) sets forth the ratio of protein to enzyme versus the modulus
of
the gum. The ratio of protein to enzyme also greatly affected the texture of
the
hydrolysate. With an increase ofpapain content, the modulus decreased. The
papain/zein
ratio was perhaps the most significant factor on the gum texture, such as
hardness,
modulus, gumminess, chewiness and springiness; it also had some impact on
cohesiveness and adhesive force. Table 3 demonstrates that the higher the
papain/zein
ratio the softer the gum.
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Table 3. Papain/zein ratio vs. modules of the gums
Modules (g/s)
control 393+/-40
0.2% papain* 232+/-I2
0.4% papain* 77+/-5
*achmty = 16U MC;U/mg
As noted above, the enzymatic zein gum base will be biodegradable. When zcin
was exposed to aerobic biodegradation pursuant to ASTM D-5209 by contacting
with
activated sewage sludge innoculum, its degradation rate was faster than both
Kraft paper
and cellulose as illustrated in Figure 1. The weight loss was 100% after about
80 days in
sewage sludge. This indicated that zein would degrade completely in less than
three
months.
The present invention can be used to construct a variety of chewing gums. The
chewing gum includes a base portion.
A variety of ingredients can be used with zein to construct the gum base.
Preferably as a gum base one or more of the following ingredients is added to
the
hydrolysate. Edible proteins such as, but not limited to, gelatin, collagen,
casein,
caseinates, gliadin, gluten, glutenin, hordein and their combinations can be
used. Protein
hydrolysates such as but not limited to hydrolyzed gelatin, hydrolyzed
collagen,
hydrolyzed gluten may also be used alone or in combination. Food grade
microbial
(fungal or bacterial) proteases or plant protease extracts which contain
tliiol proteinascs,
or serine proteinases, or carboxyl proteinases, or metalloproteinases or their
combuiations
such as but not linuted to subtilisin, chymotrypsin, trypsin, elastase,
thrombin, plasmin,
kallikrein, acrosin, papain, ficin, bromelain, actinidin, pepsin, gastricsin,
chymosin,
carboxypeptidases A and B, thermolysin, enkephalinase, coIlagenase. Humectant
such
as, but not limited to, aqueous glycol, polyol, alcohol or their combinations
such as
water, propylene glycol, glycerin, polyethylene glycol, ethanol, propanol may
also be
used in the base. Food grade polysaccharides such as, but not limited to,
native starches,
modified starches, dextrins, maltodextrin, hydroxyethylcellulosc,
hydroxypropylcellulose, dietary fibers, pectins, alginates, carrageenan,
gellan gwn,
xanthan gum, gum arabic, guar gum or other natural gums rnay be used in the
base; the
* Trademark _ 12

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
preferred polysaccharides are maltodextrin and high-conversion dextrins.
Bitterness
masking agents such as, but not limited to, malt, anethole, gelatin
hydrolysate, guar flour,
pectin, maltodextrin, sodium salts, lithium salts, phosphatidic acid,
phosphatidyl inositol,
ribonucleotide, acidic oligopecptides, lipoproteins and their combinations may
also be
used in the base. Ingestible minerals such as, but not limited to, calcium
carbonate,
calcium citrate, calcium lactate may also be used in the base. Ingestible
materials such
as, but not limited to, beeswax, candilliba wax may also be used in the base.
Edible fats
such as, but not limited to, soya, cotton seed oil, paten oil, corn oil,
peanut oil, cocoa
butter and their hydrogenates may also be used in the base. Edible acids such
as, but not
limited to, citric acid, fumaric acid, lactic acid, malic acid, tartaric acid,
ascoribc acid,
sorbic acid, succinic acid and its anhydride, adipic acid, propionic acid may
also be used
in the base. Emulsifier such as, but not limited to, monoglycerides,
diglycerides,
propylene glycol ester, lactoglycerides, succinylated monoglycerides,
acetoglycerides,
sorbitan ester, polyglcerol esters, citroglycerides, polysorbates,
polyglycerol
polyricinoleate may also be used in the base.
Preferably, the zero hydrolysate comprises approximately 25% to about 55% by
weight of the gum base.
Gum formulas may comprise from about 10 to about 95 weight percent a gum
base made in accordance with the present invention in a gum formula typically
known
to those in the art. The chewing gum may comprise softeners, sweeteners,
flavoring
agents and combinations thereof. The sweeteners often fill the role of bulking
agents in
the gum. The bulking agents generally comprise from about 5 percent to about
90
percent, preferably from about 20 percent to about 80 percent.
Softeners are added to the chewing gum in order to optimize the chewability
and
mouth feel of the gum. Softeners typically constitute from about 0.5 percent
to about
25.0 percent by weight of the chewing gum. Softeners contemplated for use in
the gum
include glycerin, lecithin and combinations thereof. Further, aqueous
sweetener solutions
such as those containing sorbitol, hydrogenated starch hydrolysates, corn
syrup and
combinations thereof may be used as softeners and bulking agents in gum. Sugar-
free
formulations are also typical.
Sugar sweeteners generally include saccharide-containing components commonly
13

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
known in the chewing gum art which comprise, but are not limited to, sucrose,
dextrose,
maltose, dextrin, dried invert sugar, fi-uctose, levulose, galactose, corn
syrup solids and
the like, alone or in any combination.
The sweetener for use in the present invention can also be used in combination
with sugarless sweeteners. Generally, sugarless sweeteners include components
with
sweetening characteristics but which are devoid of the commonly known sugars
and
comprise, but are not limited to, sugar alcohols such as sorbitol, mannitol,
xylitol,
hydrogenated starch hydrolysates, maltitol and the like, alone or in any
combination.
Depending on the particular sweetness release profile and shelf life stability
needed, bulk sweeteners of the present invention can also be used in
combination with
coated or uncoated high-intensity sweeteners or with high-intensity sweeteners
coated
with other materials and by other techniques.
High-intensity sweeteners, or artificial sweeteners and peptide sweeteners as
they
may be referred to, typically may include, but are not limited to, alitame,
thaumatin,
aspartame, sucralose, acesulfame, saccharin and dihydrochalcones. The range of
these
sweetener types in gum typically may range from about 0.02 to about 0.10
weight percent
for sweeteners such as alitame, thaumatin and dihydrochalcones, and from about
0.1 to
about 0.3 weight percent for sweeteners like aspartame, sucralose, acesulfame
and
saccharin. A flavoring agent may be present in the chewing gum in an amount
within the
range of from about 0.1 to about 10.0 weight percent and preferably from about
0.5 to
about 3.0 weight percent of the gum. The flavoring agents may comprise
essential oils,
synthetic flavors, or mixtures thereof including, but not limited to, oils
derived from
plants and fruits such as citrus oils, fruit essences, peppermint oil,
spearmint oil, clove
oil, oil of wintergreen, anise and the like. Artificial flavoring components
are also
contemplated for use in gums of the present invention. Those skilled in the
art will
recognize that natural and artificial flavoring agents may be combined in any
sensory
acceptable blend. All such flavors and flavor blends are contemplated for use
in gums
of the present invention.
Optional ingredients such as colors, emulsifiers and pharmaceutical agents may
be added to the chewing gum.
In general, chewing gum is manufactured by sequentially adding the various
14

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
chewing gum ingredients to a commercially available mixer known in the art.
After the
initial ingredients have been thoroughly mixed, the gum mass is discharged
from the
mixer and shaped into the desired form such as by rolling into sheets and
cutting into
sticks, extruded into chunks or casting into pellets.
Generally, the ingredients are mixed by first melting the gum base and adding
it
to the running mixer. The base may also be melted in the mixer itself. Color
or
emulsifiers may also be added at this time. A softener such as glycerin may
also be
added at this time, along with syrup and a portion of the bulking
agent/sweetener.
Further portions of the bulking agenbsweetener may then be added to the mixer.
A
flavoring agent is typically added with the final portion of the bulking
agent/sweetener.
A high-intensity sweetener is preferably added after the final portion of
bulking agent and
flavor have been added.
The entire mixing procedure typically takes from five to fifteen minutes, but
longer mixing times may sometimes be required. Those skilled in the art will
recognize
that many variations of the above described procedure may be followed.
By way of example, and not limitation, examples of the present invention will
now be given.
Example 1. Preparation of zero hydrolysate by enzyme complex:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 1:1 by weight. Alkaline Protease Concentrate (APC, 0.25 grams)
was then
added into the PG aqueous solution (25 grams). To a 100-ml sigma-blade mixer,
set at
60°C and 30 rpm, the zero (25 grams) and APC solution was added. After
one hour of
mixing, a homogenous, syrup-like paste was obtained. The paste was cooled to
room
temperature, and 0.5 g citric acid was added to deactivate the enzyme. The
soft paste was
then ready to be used for preparing the gums.
Example 2. Preparation of zero hydrolysate by thio protease:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Liquid papain (dried latex from papaya fruit, 165
MCU/mg,
0.4 grams ) was then added into 25 g PG aqueous solution. To a 100-ml sigma-
blade

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
mixer, set at 50°C and 30 rpm, zero (25 grams) and the above papain
solution were added.
After one hour of mixing, a homogenous, syrup-like paste was obtained. By
raising the
temperature to 90°C for one half hour, the papain was deactivated in a
closed system.
The resultant product was cooled to room temperature, and a soft solid was
ready for
preparing the gums.
16

CA 02373850 2001-12-21
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Example 3. Preparation of zero hydrolysate by serine protease:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Alcalase (2.4 AU/g, 0.25 grams) was then added
into the PG
aqueous solution (25 grams). The main component in Alcalase is subtilisin
Carlsberg
S from the selected strain of Bacillus licheniformis. To a 100-ml sigma-blade
mixer, set
at 50°C and 30 tpm, zero (25 grams) and the above Alcalase solution
were added. After
two-hours of mixing, a homogenous, syrup-like paste was obtained. The enzyme
was
inactivated for 10 minutes at 85°C before discharge. The soft paste was
ready for
preparing the gums.
Example 4. Preparation of zero hydrolysate by metalloprotease:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Neutrase (0.5 AU/g, 1.0 grams) was then added
into PG
aqueous solution (25 grams). Neutrase (0.5 AU/g) is a bacterial proteinase
produced by
a selected strain of bacillus amyloliquefaciens. To a 100-ml sigma-blade
mixer, set at
50°C and 30 rpm, zero (25 grams) and the above Neutrase solution were
added. After
two-hours of mixing, a slight phase separation was observed.
Example 5. Preparation of zero hydrolysate by exopetidase:
The propylene glycol (PG) aqueous solution was prepared by mixing PG and
water at a ratio of 3:2 by weight. Validase FP II (50,000 CFAU/g, 0.25 grams)
was then
added into the PG aqueous solution (25 grams). Validase FP II (50,000 CFAU/g)
is an
exo-peptidase produced by the controlled fermentation ofAspergillus oryzae. To
a 100-
ml sigma-blade mixer, set at 53°C and 30 rpm speed, zero (25 grams) and
the above
Validase FP II solution were added. After two and a half hours of mixing, the
blend was
discharged. It was chewable, but firmer than the hydrolysate from example 1.
17

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
Example 6. Preparation of zero hydrolysate by an endopeptidase:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Validase TSP200 (200NU/g, 0.25 grams) was then
added into
the PG aqueous solution (25 grams). Validase TSP200 (200NU/g) is an
endopeptidase
produced by the controlled fermentation of Bacillus subtilis. To a 100-ml
sigma-blade
mixer, set at 55°C and 30 rpm, zero (25 grams) and the above Validase
TSP200 solution
were added. After two and a half hours of mixing, the blend was discharged. It
was
chewable, but firmer than the hydrolysate from example 1.
Example 7. Preparation of zero hydrolysate by protease complex:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Protamex ( 1.5 AU/g, 0.25 grams) was then added
into the PG
aqueous solution. Protamex (1.5 AU/g) is a bacterial protease complex produced
by the
controlled fenmentation of Bacillus. To a 100-ml sigma-blade mixer, set at
40°C and 30
rpm, zero (25 grams) and the above Protamex solution were added. After two and
a half
hours of mixing, the blend was discharged. It was chewable, but firmer than
the
hydrolysate from example 1.
Example 8. Preparation of zero hydrolysate by protease complex:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 3:2 by weight. Flavourzyme (1000 LAPU/g, 0.25 grams) was then
added into
ml of the PG aqueous solution. Flavourzyme (1000 LAPU/g) is a fungal protease
complex produced by the fermentation of a selected strain of Aspergillus
oryzae. To a
100-ml sigma-blade mixer, set at 50°C and 30 rpm, zero (25 grams) and
the above
25 Flavourzyme solution were added. After two and a half hour mixing, phase
separation
occurred.
Example 9. Preparation of gum base from enzymatic hydrolysate of zero:
To a 100 ml sigma-blade batch mixer, set at 50°C and 60 rpm,
hydrolysates
prepared pursuant to examples 1-3 (50 grams), maltodextrin (5 grams),
hydrolyzed
gelatin (MW=15 K, 10 grams) and citric acid (0.5 grams) were added and blended
for
18

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
about two minutes. Then the mixer was re-set to 37 °C. The base was
mixed for another
60 minutes. A homogenous dough-like gum base was obtained.
Example 10. Preparation of gum base from both enzymatic hydrolysate of zero
and non-
hydrolyzed zero:
To a 100 ml sigma-blade mixer, set at 50°C and 60 rpm, hydrolysate
prepared in
Example No. 1 (50 grams), zero (1.5 grams), maltodextrin (5 grams), and
hydrolyzed
gelatin (MW=15 K, 10 grams) were added and blended for about two minutes. Then
the
mixer was re-set to 37 °C. The base was mixed for another 60 minutes. A
homogenous
dough-like gum base was obtained.
Example 11. Preparation of gum base:
To a 100 ml sigma-blade mixer, set at 55°C and 60 rpm, hydrolysate
prepared in
Example No. 2 (50 grams), glyceryl monolaurate ( 1.56 grams) and partially
hydrogenated
soy oil (7.81 grams) were added and mixed for about 10 minutes. Then,
maltodextrin (5
grams), and hydrolyzed gelatin (MW=15 K, 10 grams) were added and blended for
about
two minutes. Then the mixer was re-set to 37 °C. The base was mixed for
another 60
minutes. A homogenous dough-like gum base was obtained.
Example 12. Preparation of sugarless chewing gum from enzymatic hydrolysate of
zero:
A propylene glycol (PG) aqueous solution was prepared by mixing PG and water
at a ratio of 1:1 by weight. Alkaline Protease Concentrate (APC, 0.25 grams)
was then
added into 17 ml of PG aqueous solution. To a 100-ml sigma-blade mixer, set at
60°C
and 30 rpm, zero (25 grams) and the above APC solution were added. After one
hour of
mixing, malt powder (10 grams) was added and mixed for 40 minutes. Then the
mixer
was set at 37°C and 60 rpm. Acesulfame K (0.5 grams) and strawberry
flavor (0.5 ml)
were added and mixed for another 10 minutes before discharge.
Example 13. Preparation of sugarless chewing gum from base contained enzymatic
hydrolysate of zero and other food ingredients:
To a 100-ml sigma-blade mixer set at 60°C and 60 rpm, the base
prepared in
19

CA 02373850 2001-12-21
WO 01/01788 PCT/US00/07809
Example No. 9 (63 grams) and malt powder ( 10 grams) were added and mixed for
5
minutes. Then the mixer was re-set to 37°C and the blend was mixed for
another 40
minutes. Then, acesulfame K (0.5 grams) and strawberry flavor (0.5 ml) were
added and
mixed for another 10 minutes before discharge.
Example 14. Preparation of sugar-containing chewing gum:
To a 100-ml sigma-blade mixer at 60°C and 60 rpm, the base
prepared in
Example No. 10 (63 grams), sugar(30 grams) and malt powder (10 grams) were
added
and mixed for 5 minutes. Then the mixer was re-set to 37°C and the
blend was mixed for
another 40 minutes. Then, acesulfame K (0.5 grams) and strawberry flavor (0.5
ml) were
added and mixed for another 10 minutes.
It should be understood that various changes and modifications to the
presently
preferred embodiments described herein will be apparent to those skilled in
the art. Such
changes and modifications can be made without departing from the spirit and
scope of
the present invention and without diminishing its attendant advantages. It is
therefore
intended that such changes and modifications be covered by the appended
claims.

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Administrative Status

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Event History

Description Date
Inactive: IPC deactivated 2011-07-29
Time Limit for Reversal Expired 2007-03-26
Letter Sent 2006-03-24
Inactive: IPC from MCD 2006-03-12
Inactive: First IPC derived 2006-03-12
Inactive: IPC from MCD 2006-03-12
Grant by Issuance 2005-05-24
Inactive: Cover page published 2005-05-23
Pre-grant 2005-01-13
Inactive: Final fee received 2005-01-13
Notice of Allowance is Issued 2004-09-22
Letter Sent 2004-09-22
Notice of Allowance is Issued 2004-09-22
Inactive: Approved for allowance (AFA) 2004-09-10
Amendment Received - Voluntary Amendment 2004-06-21
Inactive: S.29 Rules - Examiner requisition 2003-12-24
Inactive: S.30(2) Rules - Examiner requisition 2003-12-24
Inactive: Cover page published 2002-06-17
Inactive: Acknowledgment of national entry - RFE 2002-06-13
Inactive: Applicant deleted 2002-06-13
Inactive: First IPC assigned 2002-06-13
Letter Sent 2002-06-13
Letter Sent 2002-06-13
Inactive: Agents merged 2002-05-08
Application Received - PCT 2002-03-27
National Entry Requirements Determined Compliant 2001-12-21
Request for Examination Requirements Determined Compliant 2001-12-21
All Requirements for Examination Determined Compliant 2001-12-21
Application Published (Open to Public Inspection) 2001-01-11

Abandonment History

There is no abandonment history.

Maintenance Fee

The last payment was received on 2005-03-03

Note : If the full payment has not been received on or before the date indicated, a further fee may be required which may be one of the following

  • the reinstatement fee;
  • the late payment fee; or
  • additional fee to reverse deemed expiry.

Patent fees are adjusted on the 1st of January every year. The amounts above are the current amounts if received by December 31 of the current year.
Please refer to the CIPO Patent Fees web page to see all current fee amounts.

Fee History

Fee Type Anniversary Year Due Date Paid Date
Registration of a document 2001-12-21
Request for examination - standard 2001-12-21
MF (application, 2nd anniv.) - standard 02 2002-03-25 2001-12-21
Basic national fee - standard 2001-12-21
MF (application, 3rd anniv.) - standard 03 2003-03-24 2003-03-11
MF (application, 4th anniv.) - standard 04 2004-03-24 2004-03-11
Final fee - standard 2005-01-13
MF (application, 5th anniv.) - standard 05 2005-03-24 2005-03-03
Owners on Record

Note: Records showing the ownership history in alphabetical order.

Current Owners on Record
WM. WRIGLEY JR. COMPANY
Past Owners on Record
JACK D. FOSTER
JINGPING LIU
WEISHENG LI
Past Owners that do not appear in the "Owners on Record" listing will appear in other documentation within the application.
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Document
Description 
Date
(yyyy-mm-dd) 
Number of pages   Size of Image (KB) 
Description 2001-12-20 20 918
Abstract 2001-12-20 1 49
Claims 2001-12-20 3 62
Drawings 2001-12-20 1 11
Description 2004-06-20 20 923
Claims 2004-06-20 3 61
Acknowledgement of Request for Examination 2002-06-12 1 179
Notice of National Entry 2002-06-12 1 203
Courtesy - Certificate of registration (related document(s)) 2002-06-12 1 114
Commissioner's Notice - Application Found Allowable 2004-09-21 1 160
Maintenance Fee Notice 2006-05-22 1 172
PCT 2001-12-20 9 318
Correspondence 2005-01-12 1 35