• Korean Journal of Food Science and Technology
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• v.35 no.2
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• pp.260-265
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• 2003

Transglutaminase (TG) was prepared from Streptomyces mobaraensis to improve texture and self-life of food. In preliminary experiments, texture of the dough was not improved due to the interference in microbial TG reaction by proteases present in the crude enzyme. Among the cation exchange resins tested for the removal of proteases, MonoPlus S 100 was the most efficient. Further purification steps with a quaternary ammonia salt resin and gel permeation chromatography effectively removed proteases from crude enzyme. Molecular weight of purified enzyme was about 38,000 on SDS-polyacrylamide gel electrophoresis. Farinograph data showed the addition of purified enzyme to wheat flour gave higher stability and lower weakness values those that of crude enzyme.

• BMB Reports
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• v.52 no.9
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• pp.554-559
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• 2019

Despite reports suggesting that tissue-resident natural killer (trNK) cells cause ischemic kidney injury, their contribution to the development of tubulointerstitial fibrosis has not been determined. This study hypothesized that the depletion of trNK cells may ameliorate renal fibrosis by affecting transglutaminase 2/syndecan-4 interactions. Aristolochic acid nephropathy (AAN) was induced in C57BL/6 mice as an experimental model of kidney fibrosis. The mice were treated with anti-asialo GM1 (ASGM1) or anti-NK1.1 antibodies to deplete NK cells. Although both ASGM1 and NK1.1 antibodies suppressed renal $NKp46^+DX5^+$ NK cells, renal $NKp46^+DX5^-$ cells were resistant to suppression by ASGM1 or NK1.1 antibodies during the development of tubulointerstitial fibrosis in the AAN-induced mouse model. Western blot analysis showed that both antibodies increased the expression of fibronectin, transglutaminase 2, and syndecan-4. These findings indicate that trNK cells played an exacerbating role in tubulointerstitial fibrosis by activating transglutaminase 2 and syndecan-4 in the AAN-induced mouse model.

• BMB Reports
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• v.34 no.2
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• pp.95-101
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• 2001

Tissue transglutaminase (TGII, $G{\alpha}h$) belongs to a family of enzymes which catalyze post-translational modification of proteins by forming isopeptides via $Ca^{2+}$-dependent reaction. Although TGII-mediated formation of isopeptides has been implicated to play a role in a variety of cellular processes, the physiological function of TGII remains unclear. In addition to this Tease activity, TGII is a guanosine triphosphatase (GTPase) which binds and hydrolyzes GTP It is now well recognized that the GTPase action of TGII regulates a receptor-mediated transmembrane signaling, functioning as a signal transducer of the receptor. This TGII function signifies that TGII is a new class of GTP-binding regulatory protein (G-protein) that differs from "Classical" heterotrimeric G-proteins. Regulation of enzyme is an important biological process for maintaining cell integrity. This review summarizes the recent development in regulation of TGII that may help for the better understanding of this unique enzyme. Since activation and inactivation of GTPase of TGII are similar to the heterotrimeric G-proteins, the regulation of heterotrimeric G-protein in the transmembrane signaling is also discussed.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.1
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• pp.106-110
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• 2002

The purpose of this study was to examine the effect of different levels of crude pig plasma transglutaminase (TGase) on the quality of milk curd. Different levels (0, 0.1, 0.2, 0.4, 0.8 and 1.0%) of crude pig plasma TGase was added to fresh milk, individually, and then incubated at $35^{\circ}C$. The time of milk curdling was recorded. Simultaneously, rheological properties, L value and microstructure of the samples were measured and observed. The results showed that the time of milk curdling decreased and the curd strength of milk curd increased with increasing of TGase (p<0.05). The softness of milk curd had the highest value when 0.8% TGase was added (p<0.05). However, L value of milk curds was not significantly different among all treatments. The microstructure of milk curd observed by scanning electron microscopy (SEM) became more dense with TGase level increased.

• Food Science of Animal Resources
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• v.30 no.5
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• pp.746-754
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• 2010

Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono-$\delta$-lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.

• Food Science and Biotechnology
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• v.14 no.5
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• pp.608-613
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• 2005

Effects of transglutaminase (TG) on physicochemical properties of dough prepared with 20% resistant starch (RS)-added wheat flour were investigated. RS levels of wheat flours added with native wheat starch (NS), Hi-maize (RS2), retrograded (RS3), and cross-linked (RS4) wheat starches were 2.97, 11.88, 5.79, and 9.09%, respectively. Peak viscosity of NS-added flour was higher, whereas setback was lower, than those added with other resistant starches. TG had no effect on pasting behaviors of RS-added flours. Water absorption ranged from 66.5 to 79.0%, and development time increased with RS addition. TG increased tensile strength of dough after fermentation and bread volume, due to well-developed gluten network resulting from cross-linking facilitated by TG Addition of TG decreased hardness of baguettes, with RS2-added baguette showing lowest value. These results indicate addition of TG enhanced eating quality of RS-added breads.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.8
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• pp.1111-1117
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• 2009

Effect of Rubus coreanum Miquel and Opuntia ficus-indica var. saboten in combination with chicken breast and wheat gluten on functional properties and physicochemical characteristics during processing of cooked noodles were investigated. These studies were carried out to investigate functional properties of Rubus coreanum Miquel and Opuntia ficus-indica var. saboten by the antioxidant ability. Antioxidant activities were evaluated by electron donating, xanthine oxidase inhibition rate and contents of total polyphenols. Overall, the antioxidant activities of hot water extracts were a little higher than those of ethanol extracts. Also, the antioxidant abilities at the concentration of 1,000 ppm in hot water extracts were higher than those of ethanol extracts by the determination of total polyphenol content and DPPH, which showed 150.25 mg% in extracts of Rubus coreanum Miquel and showed 69.36% in extracts of Opuntia ficus-indica var. saboten. The effects on processing characteristics of cooked noodles were investigated in combination with transglutaminase (TGase), plant extracts, wheat gluten and chicken breast. Cooking time was very short as 340 second in CB (cooked breast), compared to other treatments. In contrast, NCB (non cooked breast) took a longer time as 779 second. Also, CB was higher than NCB, which showed 146.3% in CB and 61.5% in NCB in water absorption ratio during cooking of noodles. Tubidity of soup was the lowest at 0.240 in NCBT (non cooked breast transglutaminase), which means the lowest loss of solid in noodle during cooking. In case of treatment of TGase, overall texture properties were higher than other samples in hardness, cohesivness, springness and gumminess. In sensory evaluations, cooked noodles treated with TGase showed a higher percentage of overall acceptability than other treatments.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.65-66
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• 2003

The cause of Huntington's disease (HD) is a pathological expansion of the polyglutamine domain within the N-terminal region of huntingtin. Neuronal aggregates composed of mutant huntingtin within certain neuronal populations are a characteristic hallmark of HD. Because tissue transglutaminase (tTG) cross-links proteins into aggregates and polypeptide-bound glutamines are primary determining factors for tTG-catalyzed reactions, it has been hypothesized that tTG may contribute to the formation of aggregates. (omitted)

• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.165.2-165
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• 1996

No Abstract, See Full Text

• Korean Journal of Food Science and Technology
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• v.37 no.3
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• pp.345-351
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• 2005

Physicochemical properties and functionalities of sodium caseinate, whey protein, skim milk, and whole milk with or without transglutaminase (TGase, 200 : 1) at $38^{\circ}C$ were determined. After crosslinking by TGase, whey protein was effective in improving heat stability compared to native protein at over $70^{\circ}C$. Whole milk was stable with lower turbidity compared to native solution. Whey protein showed low hydrolysis degree, fewer than sodium caseinate, during early activation time and increased slightly thereafter Emulsifying activities of sodium caseinate at pH 2 and 8, and whey protein at pH 7 and 8 improved. Emulsion stability of sodium caseinate improved at entire pH range studied. Foam expansion and foam stability of samples improved with TGase-treatment. Viscosities of TGase-treated samples were higher than those of untreated ones.