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Recent Patents on Transglutaminase Production

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166 Recent Patents on Biotechnology 2009, 3, 166-174

Recent Patents on Transglutaminase Production and Applications: A Brief

Review
Mireya Santos* and J.M. Torn

Centre of Research in Agrogenomics (CRAG)- CSIC-IRTA-UAB. Department of Molecular Genetics. Jordi Girona 18-
24. 08034 Barcelona. Spain

Received: April 1, 2009; Accepted: May 18, 2009; Revised: June 26, 2009
Abstract: The transglutaminases (TGase; EC2.3.2.13) (R-glutaminyl-peptide-aminase-
-glutamyltransferase) are a family
of enzymes that catalyse post-translational modifications in proteins, producing covalent amide bonds between a primary
amine group in a polyamine or lysine (amine donor), and a
-carboxamide group of the glutamyl residue of some proteins
(amine receptor). These enzymes were detected for the first time in animals, where they modify structural proteins, and
are widely distributed in bacteria, animals, and plants. Of all the reactions that are catalysed by TGases, protein cross
linking has probably attracted the greatest interest owing the industrial applications of these catalytic reactions.
A review of the patents related to the different cloned TGases and its putative applications in medicine, food processing,
and other applications as polymer obtaining, etc., is presented here. Due to the widespread number of recently published
patents about this enzyme, a classification in relation to a) species origin and b) application field, is presented.
Keywords: Transglutaminase enzyme, cross-linking, gene cloning, structural proteins, lysine, polyamines, biomedicine,
biomaterials, food processing, antibodies, alternative technologies, wool processing, leather processing.

INTRODUCTION The cloning of different TGases has clarified to some

Description and Presence of TGase in the Different
Living Organisms
Transsglutaminases (TGase; EC2.3.2.13) (R-glutaminyl-
peptide-aminase-
-glutamyltransferase) are a family of
enzymes that catalyse post-translational modifications in
proteins, producing covalent amide bonds between a primary
amine group in a polyamine or lysine (amine donor), and a
-
carboxamide group of the glutamyl residue of some proteins
(amine acceptor) see Fig. (1). The results of this activity are
as follows: a) modification of the conformation of the pro-
tein; and b) other more extensive conformation changes
resulting from bonding between the same protein and
between different proteins in order to form high molecular
weight conjugates. TGases are widely distributed in
organisms as different human, bacteria, nematodes, yeasts,
algae, plants, and lower vertebrates. This would indicate that
these enzymes play a fundamental role in biological
processes [1]. A particular feature of the enzyme is that most
of TGases require Ca+2 for their catalytic activity. It has been
demonstrated that there is a great difference between protein
sequence characteristics [2]; as one example, the two TGases
cloned in bacteria (Bacillus subtillis and Streptoverticillium
sp.) have no homologies with any known family of enzymes
or other TGases. Nine TGases have been described in
humans that differ in terms of specific substrates and which
have revealed a high degree of sequence homology. The best
known is human blood coagulation factor XIII (fibrin-
stabilizing factor) [3]. Four transglutaminases are also
known to be expressed in the human epidermis.
*Address correspondence to this author at the Centre of Research in
Agrogenomics (CRAG)- CSIC-IRTA-UAB. Department of Molecular
Genetics. Jordi Girona 18-24. 08034 Barcelona. Spain; Tel: 34 3 4006123;
Fax: 34 3 2045904; E-mail: mireya.santos@cid.csic.es
extent the involvement of these enzymes in important cell
differentiation processes, tissue stabilization, and program-
med cell death [4-6]. Some TGases also appear to be
implicated in neurodegenerative diseases (Alzheimers and
Huntingtons), cancer, celiac disease, skin disorders, etc. and
so these enzymes are of great interest in clinical trials. Since
1997 it has been known that TG2 is the most important
autoantigen in celiac disease and its use as a marker of this
disease is being studied. The different types of TGases were
widely reviewed by Lorand and Graham in 2003 [7].
Enzyme Substrates
As for the substrates on which the enzyme acts, although
in some cases the modifications directed by the TGases have
been demonstrated indirectly, there is an increasing amount
of data that has been confirmed with intact cells or live
tissues. In these studies it has been observed that, apart from
catalysing modifications of proteins, TGases are also capable
of other functions. An example is human TG2, a multi-
functional protein with TGase activity triggered by calcium;
it is inhibited by binding to GTP and a GTPase receptor
signaling activity which requires binding to GTP. The
enzyme also functions, therefore, as a G protein that parti-
cipates in signalling processes. Nonetheless, despite impor-
tant advances in biochemical and structural studies of this
protein, its physiological role remains uncertain [7].
TGase Importance in the Plant Kingdom
Although preliminary data on the existence of plant
TGases were published many years ago [8], much more
recent and not exhaustive is the knowledge about its physio-
logical role. The differences on the level and content of the
studies in plants with respect to other species (including

1872-2083/09 $100.00+.00 2009 Bentham Science Publishers Ltd.

Transglutaminase Patents
Fig. (1). Two types of transglutaminase catalysed reactions: cross-linking of polyamine or lysine to protein glutamine residues, and cross-
linking of proteins.
mammals) are important. However, owing the interest of
plants in a significant number of physiological, metabolic
and biotechnological applications, these studies became
more and more interesting. By the knowing data, is possible
to asseverate that, the TGase presence in specific plant cell
compartments and the type of substrates suggest that it
should have specific and important functions. Briefly, we
can say that TGases operate mainly in the processes of
growth and cell differentiation, although, as in animals,
plants are also associated with programmed cell death
processes [9]. Most of the plant TGase studies have focused
on aspects related to the biochemical activity, substrates and
cell/tissue localization, but data on their functional role in
morphogenesis, photosynthesis, cell death, etc., are only
partial [10-12]. One of the reasons for this problem may be
that the only plant TGase gene cloned is that of the plastidial
TGase (TGZ) [13]. In contrast, some of the mammalian
TGases genes were cloned some years ago. The most
abundant data show the relationship of certain TGases with
chloroplasts. It has been published that the LHCII antenna
proteins are substrates of TGase activity in isolated
chloroplasts [11] and there has been co-localised with TGase
in plant developing chloroplasts [14]. The enzyme activity
increases in the presence of light [12, 15], and after the first
cloning of two maize cDNAs encoding chloroplast TGases
[13, 16] it has been confirmed that the TGase mRNA
depends on the plant illumination period and on the stage of
chloroplast development [17]. Finally, tobacco plants had
been transformed with the maize plastidial TGase gene (tgz)
Recent Patents on Biotechnology 2009, Vol. 3, No. 3 167
and significant variations in the grana appression pattern and
in many photosynthesis-related parameters are detected [18].
Pathology Implications and Biotechnological
Applications
Numerous pathologies have been related to changes in
the regulation of the expression of this enzyme, as there are
disorders in the blood coagulation, cancer, neurodegene-
rative diseases, etc. [19-22]. TGases are also present in
nervous terminals, and recognize the sinapsine I as a subs-
tratum, a phosphoprotein involved in neurotransmission.
Recently, the role of the TGase II in the formation of the
covalent linkage intra or intermolecular, during the apoptosis
[23, 24] and in the formation of aggregates of high molecular
weight of the enzyme substratum aconinase in mitocondria,
which loses his activity in samples of rat brain in
Huntingtons disease had been demonstrated [25]. These
enzymes are essential for the understanding of the aetiology
of diverse hereditary blood and skin diseases, as well as of
several autoimmune and degenerative responses.
With respect to its biotechnological applications, owing
its protein cross linking and transamidation characteristics, it
is not surprising that this group of enzymes has been
exploited like biocatalyzers in a wide scale of commercial
sectors like food sector textile industry, cosmetics, and many
others [26-28], If we attend on the number of patents of
applications in which TGases are implicated, we meet three
hundred sixty in the decade from 1991 to 2001. In the actual
168 Recent Patents on Biotechnology 2009, Vol. 3, No. 3 Santos and Torn

decade, the number of TGase registered Patents have been
multiplied by ten times with respect to that of the past
decade.
The first over-expressed TGase for food application was
carried out in Streptoverticillium sp. bacteria by
Ajinomoto, that patented the procedure and the different
later progresses of this initial protocol [29]. This microbial
TGases are characterized for its non-calcium dependence.
The same company posses another similar patent, using
Crassostrea gigas transformation [30]. With the same aim,
our group has patented the DNA sequence and applications
of plastidial maize TGase [16], the first TGase patented in
plants.
In the present review, a commented patent classification
on TGase cloning and applications is presented. Owing the
great quantity and variants of published patents including
this enzyme, only the most significant references with
respect to each subject are presented.
Patents on Genes Coding for TGases
In Table 1, the most significant Patents including TGase-
codifing genes are presented. As can be seen, different genes
coding for TGase had been patented until present, although
these are not all the discovered TGase-codifing genes. The
different patents are commented and referenced.
The first TGase sequence patented was that of the
Japanese oyster [31]. From the microbial genes, the genus
Streptomices and Streptoverticillium are the most studied and
patented [29, 32-35]. In this aspect, Steeptoverticillium m. is
the specie from which the cited Ajinomoto patent [29] is
based to the production of microbial TGase (MTG) for its
use as food additive in a very elevated number of appli-
cations. Furthermore, TGase from Micrococcus, Clostridium,
Turolpsis, Rhizopus and Monascus [30, 36, 37], Bacillus s.
[37] and Streptomices mobaerensis [32] are also registered.
From fungi, only Oomycetes and Actinomicetes TGases
had been cloned and patented [38,39].
In the case of nematodes, the DNA sequence of
Dirofilaria i. TGase must be underlined [40]. There is also a
gene coding TGase from fish (Theragra ch.) [41].
Into the plants, only the maize DNA TGase sequence has
been patented [16].
Due to its applications in biomedicine, the cloning and
patenting of human TGases are of special interest. In this

Table 1. Patents on Different TGase Codifing Genes The Author References are Ordered by Type of Patent Document and by Year
of Publication. Complete References are Listed on the References Chapter

Document Number Abbreviate Title Genus/Species/Class Authors

US6414115 Parasitic nematode TGase proteins Dirofilaria immitis Chandrashekar, R. Mehta, K. 1992

US5514579 Human TGase Human prostatic and placental cells O'hara, P.J. et al. 1992

US5726051 TGase gene Human. erytrolekemia cells Fraij, B.M. et al. 1994

US4278765 Transglutaminase originating in japanese oyster Japanese oyster Ajinomoto co. inc. et al. 1995

US5840295 Nerve-derived TGase enzyme Mamamlian central nervous system Schwartz, M. and Eitan, S.1995

US5607849 Gene encoding TGase from fish Theragra chalcogramma Yasueda, H. et al. 1995

US6472182 Process for producing TGase from microorganisms Micrococcus, Clostridium, Kobayashi, K. et al. 1997
Torulopsis, Monascus, Rhizopus

US5736356 TGase originating from Crassostrea g. Crassostrea gigas Sano, K. et al. 1998

US5804102 Process for producing microbial TGase Streptoverticillium sp. Yokoyama, K. et al. 1998

US6190896 Active human cellular TGase Human. Red blood Fraij, B.M. 1999

US5731183 Bacillus-derived TGase Bacillus subtilis Kobayashi, K. et al. 1999

US20020187525 Method of producing microbialTGase Actynomicetes Taguchi, S. and Momose, H. 2002

US20030059914 TGase from oomycetes Oomycetes Bech, L. et al. 2003

US20030082746 Process for producing TGase Streptoverticillum cinamoneum Kikuchi, Y. et al. 2003

US20030113407 TGase gene of Streptovert. ladakanum Streptoverticillum ladakanum Lin, Y. et al. 2003

US20040072186 TGase gene products Human. Keratinocyte cells Aeschlimann, D. et al. 2004

US77262057 Maize nucleotide seq. coding for a protein with Zea mays L. Torn et al. 2004
TGase activity and use

US20050064571 TGase Streptoverticillum platensis Lin, Y. et al. 2005

US20050221302 Tissue TGase Human. Skin cells Powell, M. et al. 2005

US20060035366 TGase producing strain Streptomices mobaerensis Yuuki, K.and Washizu, K. 2006
Transglutaminase Patents
sense, that of prostatic and placental cells [42], the
erytrolekemia cells [43], central nervous system cells [44],
active red blood TGase gene [45], keratinocyte cells [46],
and skin cells [47], have been obtained and patented.
With respect to sequence similarities, as commented
before although the catalytic triade is conserved into the
TGase sequenced genes, the amino acid sequence of this
enzyme do not present a great homology between the diffe-
rent species. In fact, there are different published classifi-
cations of the TGase family [2, 7]. In Fig. (2), a phylogenetic
relationship between the most important cloned TGases, the
majority of them cited in Table 1 is presented.
TGase Application Patents
Table 2 shows the most relevant patents on TGase appli-
cations into different fields. In the following paragraphs, the
different patents are commented and referenced. Likewise,
Fig. (3) shows a schematic representation of the different
TGase applications described later on.
Medicine and Pharmaceutics
One of the most abundant group of TGase application
patents is that of the TGase-inhibitor products. Likewise,
dryness treatment by hialuronic acid [48], glucosamine [109]
Fig. (2). Phylogenetic relationship between the most important sequenced TGases. Villalobos et al. Gene 2004.
Recent Patents on Biotechnology 2009, Vol. 3, No. 3 169
sulphonamide or imidazol [50,51], and azole salts [52], are
patented for their use in the inactivation of different TGases.
In particular, some of these products must be used in human
diseases characterized by TGase over-expression like celiac
disease, Huntington and Alzheimer [53,54], cancer-targeting
[55], acne [56], microfilaria development [57], and scar
tissue treatment [58]. There are also other applications that
inhibit TGase activity [59]. Furthermore, TGase inhibitors
may be used for food applications, as in the case of milk
[60].
Another important TGase patent application field is that
of the biomedicine and biomaterials. This is the case of
TGase utilisation in: collagen cross linking to obtain
biomedical implants [61-64], prostate disease diagnosis [65],
attaching agents to body tissue [66], polymerization of NF-
kB factor in treated cells [49], facilitate cancer cells [67],
curl retention in hair and lashes [68, 69], enzimatically
tanning skins [70], haemoglobin cross linking [71], and
hydro gels [72].
Finally, the production of anti-TGase antibodies for its
medical and/or industrial applications, in saliva [73], inhi-
bition of neuronal cells dead [74], celiac disease diagnosis
[75,76], immunosuppressant fabrication [77], or prevention
of mammalian infections [78], may be also underlined.
170 Recent Patents on Biotechnology 2009, Vol. 3, No. 3 Santos and Torn

Table 2. Patents on TGase Applications. The Author References are Ordered by Type of Patent Document and by Year of
Publication. Complete References are Listed on the References Chapter

Document Number Abbreviate Title Product Applications Author/s

US4968713 Certain imidazole compounds as TGase Factor XIII TGase inhibition by imidazole Baldwin, J.J. et al. 1990
inhibitors comp

US4929630 TGase inhibitors Inhibition of epidermal transglutaminase and Castelhano, A. et al. 1990
the treatment of acne

US4917904 Process for the production of TGase-containing TGase is added to food material to improve Wakameda, A. et al.1990
food having improved tesxture texture

US5047416 Triazole compounds and their use as TGase Azole and azolium salts as TGase inhibitors Remy, D. C. et al. 1991
inhibitors

US5124358 Effect of TGase inhibition on microfilariae Blocking macrofilariae production in Kapil, M. et al. 1992
development and macrofilariae viability nematodes by a TGase inhibitor (MDC)

US5143925 Alteration of rate and character of hair growth Skin application of an inhibitor of TGase Shander, D. et al. 1992

US5525336 Cosmetic containing comeocyte proteins and Cosmetic ingredients cross-linked with Green, H.Dijan, P. 1996
TGase and method of application proteins

US5549904 Biological adhesive composition and method TGase in aqueous carrier pharmaceutically Juergensen, K. et al. 1996
of promoting adhesion between tissues acceptable to make biological adhesive

US5563047 Method for crosslinking haemoglobin Haemoglobin crosslinked by TGase and Petersen, B. R. 1996
inactivation

US5531795 Method for casein finishing of leather Dry of leather by TGase added to a casein Rasmussen, L. et al. 1996
solution

US5681598 Process for producing cheese using TGase Production of natural cheese Kuraishi, C. et al. 1997

US5686124 Method for reestructuration of raw meat by Reestructuration of raw meet Slashed, Ll. A. et al. 1997
TGase addition

US5695753 TGases as immunosupressants Fabrication of immunosupressants Stief, T. et al. 1997

US5882864 Biomarkers and targets for diagnosis, Test samples from prostate tissue or serum An, G. et al. 1999
prognosis and management of prostate disease with a marker selected from prostate-specific
TGase

US5885982 Use of TGase inhibitor for the treatment of Application to a scar tissue of a non-toxic Dolynchuk, K.N. et al. 1999
scar tissue amine inhibitor of TGase

US5928689 Method for treating PSE meat with TGase Improving quality of pale, soft and exudate Milkowski, A. et al. 1999
meat

US5858423 Chewing gum comp. cont. gliadin and TGase Food chewing gum composition with TGase Yajima,M., Katahira,R. 1999

US6432458 Enzyme preparation and process for producing Application of TGase, carbonate and/or a Yamazaki, K. et al. 1999
noodles reducing agent, in addition to cereal
materials

US6114119 TGase and gene encoding same Degenerate-oligonucleotides to obtain new Aeschlimann. D. and
TGase genes Mosher, D. 2000

US6051033 Method for enzymatic treatment of wool TGase improving shrink resistance, strength, Mcdevitt J.P. and Winkler, J.
etc. 2000

US6030821 Stabilized TGase and enzyme prep. cont. the TGase stabilization Soeda, T. et al. 2000
same

US6063408 Process of making chocolate Stable chocolate, preventing blooming by Yamazaki, K.Soeda, T. 2000
TGase

US6190879 Microbial TGases, their production and use TGase activity assay based on hydroxamate Bech, L. et al. 2001
Transglutaminase Patents Recent Patents on Biotechnology 2009, Vol. 3, No. 3 171

(Table 2) Contd.

Document Number Abbreviate Title Product Applications Author/s

US6200789 Enzymatic treatment of proteinaceous animal Useful animal by-products by TGase Marmer, W.N. et al. 2001
by-product materials to impart cohesion and incubation
strength

US6416797 Process for making wheyless cream cheese Using of whey nutrients to make cream Han, Xiao-qing et al. 2002
using TGase cheese

US6388056 Inhibition of TGase-mediated microbial Prevention or treat.of mammalian Sundstrom, P. et al. 2002
interaction with a mammalian host microorganism infections by TGase
substrates or antibodies

US6491957 Chinese snacks Adhesive proteinic with TGase Terazaki, H. et al. 2002

US6517874 Utilization of TGase for production of backed TGase- containing flour for backed goods Schuhmann, F. 2003
products with a low wheat content production

EP1200827 Diagnosis of gluten sensitive enteropathy and Testing the sample for antibodies against Sardy, M. et al. 2004
other autoimmunopathies human TGases

US6794414 Methods and compositions for treating diseases Treatment of diseases mediated by TGase: Steinman, L. 2004
mediated by TGase activity Huntingtons, spinobulbar atrophy, inflam.
etc.

US6770310 Pickle solution including TGase, method of Pickle preparation with proteins, TGase, and Susa, Y. et al. 2004
making and using ammonium salt as TGase suppressor

US6958148 Linkage of agents to body tissue using Methods and kits to attaching agents to a Green, H. et al. 2005
microparticles and TGase body tissue surface

US7108876 Shaped cheese reconstruction with TGase Improving cheese quality Grindstaff, D. et al. 2006

US7090971 TGase has intrinsic kinase activity Compounds identific.modulating TG-kinase Mishra, S. and Murphy, L.
activity 2006

US20080003292 Nanoparticles and meth. for production thereof Aqueous gelatin cross-linked by TGase or Ahlers, M. et al. 2008
laccase.

US20080279844 Method for treating cancer targeting TGase TGase inhibition for treating cancer Mehta, K. and Verma, A.
2008

US20080038760 Method for detecting anti-TGase antibodies Detecting anti-TGase antibodies in saliva Mascart, F.Ocmant, A. 2008

US20080305517 TGase corsslinked collagen biomaterial for Production of improved collagen biomaterial Griffin, M. et al. 2008
medical implant materials to obtain biomedical implants

US20080226769 Process for producing soybean protein and TGase is used to improve both the gel Kato, H. 2008
processed meat food using the soybean protein property and the emulsifying property

US20070105770 TGase mediated conjugation of peptides Peptides conjugation Johansen, N.L. et al. 2007

US20070202213 Method for producing TGase composition Products containing protease-TGase Ishida, R., Nakagoshi. H.
2007

US20070123462 Effect of tissue TGase on beta-amyloid- Inhibition of neuronal cells dead by Cerione, R. A. et al. 2007
induced apoptosis inhibiting human tissue TGase

US20060029943 Glucosamine and deriv. useful as TG inhibitors Inhibitory activity against TGase Kim, S.Y. 2006

US20060183759 Tissue TGase inhibitors Celiac spru, Alzheimers, Huntingtons Stein, R.L. et al. 2006
diseases

US20060104966 TGase linkage of agents to tissue Attaching agents to body tissue Green, H. et al. 2006

US20060275872 Method for modif. TGases from Prep. mutant TGases in basis of MTG Kashiwagi, T. et al. 2006
microorganisms structure
172 Recent Patents on Biotechnology 2009, Vol. 3, No. 3 Santos and Torn

(Table 2) Contd.

Document Number Abbreviate Title Product Applications Author/s

US20060286608 Method for screening TG2 inhibitor or NF-kB factor polymerization in treated cells Kim, S.Y. 2006
activator

US20060015959 Transgenic animals expressing TGase II Animals and cells harbouring TGII gene Bian, F. et al. 2006

US20050031603 Food grade TGase inhibitors and uses TGase inhibitor from milk and applications Hubertus D. et al. 2005

US20060094643 Compositions of hyaluronic acid and meth.of Treatment of dryness by hyaluronic acid Svirkin, Y. et al. 2006
use conjugates

US20040030408 Medical implant materials Mam. TGase and a polymer for Griffin, M. et al. 2004
med.implants

US20040266690 Formation of novel EPO conjugates using Covalently conjugation of EPO molecules Pool, Ch. 2004
TGase

US20040185147 TGase soy fish and meat products and analogs Process of preparing a TGase-coupled veg. Hwang, D. Ch. 2004
protein

US20040241284 Meth. for prod. TGase-cross-linked proteins of Producing cross-linked vegetable proteins Schaefer, Ch. and Funda, E.
vegetable origin, protein gels and their use 2004

US20040166221 Gummi candy and production thereof Gummi material and granules adhered by Hashimoto, J. 2004
TGase

US20040265951 Injectable and bioadhesive polymeric Biomimetic gels using a TGase to cross-link Messersmith, P.B. et al. 2004
hydrogels and related methods of enzymatic polymer-peptide conjugates of rational
preparation design

US20040259176 Structural basis for the guanine nucleotide- Facilitate death of cancer cells by inhibition Cerione, R. A. et al. 2004
binding activity of tissue TGase and its of tissue TGase
regulation of transamidation activity

US20040151685 Method of curl retention in hair and lashes Applying a TGase to the keratinous material Popescu, L.C. et al. 2004
TGase activity inhibition

US20030225007 Sulfonamide deriv. of 3-sustituted imidazol Chemical compounds that inhibit TGase Tam, T. F. et al. 2003
benzimidazole as inhib. fibrin cross-linked
TGase

US20020132776 Inhibitors of TGase Chemical compounds that inhibit TGase Fuchsbauer, H. et al. 2002
activity

US20020006633 Assay for anti-TGase antibodies detection Non-instrumental assay based on Sorell, G.L. and Acevedo,
useful in celiac disease diagnosis immunochromatographic assay principles C.B. 2002

US20020155524 Agent and method for enzymatically tanning Collagen crosslink in the hide by TGase Feigel, T. et al. 2002
skins

Food Industry improve wool resistance [96], nanoparticles of aqueous gela-

tine cross-linked by TGase [97], methods of peptide conju-
With respect to the application of TGase in food
gation [98], linkage of agents to tissue [99,100], transgenic
derivatives or additives, there are important patents on soy- animals expressing TG2 [101], degenerate oligonucleotides
bean protein and processing meat food [79-84], noodle
to obtain new TGase genes [102], TGase activity measure
production [85], gummy candy [86], improving cheese qua-
protocols [103], compounds to identify kinase activity of
lity [87-89], chewing gum obtaining [90], backed products
TGase [104], TGase stabilization systems [105], dry of
manufacturing with a low wheat content [91], improving
leather [106], obtention of protease-TGases [107], and
food texture [92], adhesive proteic production for snacks
cosmetic ingredients TGase-added [108].
[93], pickle preparation [94], and stable chocolate obtaining
[95].
CURRENT & FUTURE DEVELOPMENTS
Other Applications
From all the presented information, the importance of
In this section, we can consider a group of different this enzyme and its numerous applications in the different
patents, including: enzymatic treatment with TGase to described fields became evident.
Transglutaminase Patents
Fig. (3). Transglutaminase industrial applications
However, it may be also underlined that biochemical and
molecular basic research to deep on the different roles and
functionality of transglutaminase, substrate dependence, etc.,
into the different organisms and cell systems, are of funda-
mental importance. The more these factors will be known,
the better its implication in the different studied phenomena
may facilitate new and productive applications.
ACKNOWLEDGEMENTS
Authors thanks to www.freepatentsonline.com for the
information about the included patents.
CONFLICT OF INTEREST
Authors declare that no patents are cited by authors
which are in various stages of legal litigation. Authors have
no conflict of interest to declare.
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