• The Korean Journal of Mycology
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• v.36 no.1
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• pp.93-97
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• 2008

A $Ca^{2+}-independent$ microbial transglutaminase (mTGase) from the actinomycete Streptomyces mobaraensis IFO13819 is a useful enzyme in the food industry. It is consists 406 amino acid residues, which comprised leader and pro region of 75 amino acid residues and the structure region of 331 amino acid residues. Pro and structure gene of TGase were cloned into the yeast shuttle vector pYAEG-TER and then used to transform Saccharomyces cerevisiae 2805. Expression of mTGase in recombinant was confirmed with Northern hybridization and the maximal activity of TGase was shown 26 mU/ml.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.9
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• pp.1434-1442
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• 2005

The Present study was attempted to investigate the Possibility of modification of functional properties of the rice flour by crosslinking proteins using microbial transglutaminase (mTGase) derived from a variant of Streptoverticillium sp. MTGase was added at various levels (3,000, 5,000, 7,000 and 10,000 ppm) during making noodles mixed with the rice flour. Mixograph and farinograph showed that imported wheat flour (IWF) had strong dough stability, while the rice flour showed very weak dough strength. However addition of mTGase (3,000, 5,000 and 7,000 ppm) resulted in improvement of dough stability of the rice flour. Texture profile analysis (TPA) results indicated that most of texture parameters (gumminess, chewiness and hardness) of cooked noodles prepared from the rice flour were significantly lower than those of noodles prepared from IWF. However, by addition of mTGase (at the levels of 3,000, 5,000, 7,000 ppm) dough stability and all the TPA values and sensory score (at the level of 7,000 ppm mTGase) on chewiness and hardness of cooked noodles made with $30\%$ rice flour were improved significantly. These results suggest that dough stability and texture of rice noodles as well as sensory characteristics could be improved by addition of mTGase to the rice flour.

• 축산식품과학과 산업
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• v.1 no.1
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• pp.42-50
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• 2012

• 축산식품과학과 산업
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• v.4 no.2
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• pp.45-55
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• 2015

• The Journal of Korean Medicine
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• v.25 no.4
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• pp.188-199
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• 2004

Transglutaminase 2 (TGase 2) is an enzyme that is widely used in many biological systems for generic tissue stabilization purposes or immediate defenses for wounds. Many reports have showed that TGase 2 is aberrantly activated in tissues and cells and contributes to a variety of diseases, including neurodegenerative diseases and autoimmune diseases. In most cases, the TGase 2 appears to be a factor in the formation of inappropriate proteinaceous aggregates that may be cytotoxic. However, in other cases such as celiac disease, arthritis, lupus, amyotrophic lateral sclerosis, TGase 2 is involved in the generation of autoantibodies. This suggests the possibility that the inappropriate expression and/or presentation of TGase 2 to T cells might contribute to these diseases in genetically predisposed individuals. Others and we have found that TGase 2 expression is also increased in the inflammation process. We also demonstrated reverse of inflammation by TGase inhibition. Furthermore we discovered the genuine role of TGase 2 in immune cell activation. Increase of TGase activity induces or exacerbates inflammation via NF-κB activation without I-κBα kinase signalings. This review will examine a possibility of TGase inhibitors as therapeutic agents in a variety of inflammatory diseases.

• Korean Journal of Food Science and Technology
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• v.33 no.4
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• pp.474-478
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• 2001

Transglutaminase(TGase) 첨가가 튀긴 어묵의 레올로지 특성에 미치는 영향이 평가되었다. 최적의 TGase 함량과 setting시간은 저온$(25^{\circ}C)$ setting에서는 0.1%와 180분이었고, 고온$(40^{\circ}C)$ setting에서는 0.3%와 80분으로 각각 결정되었다. 각각의 최적조건에서의 겔 강도는 $25^{\circ}C$에서는 TGase를 첨가한 겔이 첨가하지 않은 겔보다 최대 750(g cm)도 증가했으며, $40^{\circ}C$에서는 약 800(g cm)정도의 증가를 보여주었다. 동적 점탄성의 setting 측정 결과로부터 TGase 첨가 시료는 $25^{\circ}C$인 경우 G#과 G@ 값이 각각 1.0 kPa과 0.5 kPa 정도 증가하는 것으로 나타났으며, $40^{\circ}C$ 경우는 G#과 G@ 값이 각각 15 kPa과 2.2 kPa 정도 증가함을 보여 주었다. 동적 점탄성의 가열-냉각 측정 결과에서도 $25^{\circ}C$와 $40^{\circ}C$ setting 모두에서 G#, G@ 값이 $5{\sim}15\;kPa$ 정도 증가함을 나타났다.

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.29 no.2
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• pp.86-94
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• 2003

It has been known that transglutaminase C (TGase C, TGase II) is directly participated in the DNA organization of chromosome, and affects the cellular processes such as proliferation, differentiation, and apoptosis of cells, but still not known what mechanism is working on. In this study, the cytogenetic and the immunohistochemical methods were used to observe the TGase C expression in the nuclear chromosome of the proliferating cells, especially in mitotic stage. The human gastric adenocarcinoma (SNU-1) cell line was used for immunohistochemistry and antisense inhibition study in vitro. The present study was also aimed to disclose the efficiency of antisense inhibition by using antisense oligonucleotide DNA labeled with fluorescence, and found that anti-TGase C probe was diffusely infiltrated into the cytoplasm and the nucleus of the cell. By the antisense inhibition the nuclei of SNU-1 cells became rough nuclear shape, as they were greatly reduced in TGase C immunoreactivity both for the normal and apoptotic SNU-1 cells. However, it is clearly presumed that the TGase C directly interacts with the chromosome of SNU-1 cells and it may play an important role in the division and organization of the chromosome during the mitotic stage.

• Food Science of Animal Resources
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• v.30 no.6
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• pp.886-895
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• 2010

The level of fat and salt can affect the product quality and storage stability of processed meats. Additionally, consumers' demands require dietary guidelines for developing low-fat/salt functional foods. Microbial transglutaminase (MTGase), which enhances textural properties by catalyzing protein-protein cross-linkages, was introduced to develop healthier lowfat/salt meat products. The potential possibilities of low-fat/salt processed meats were reviewed under optimal conditions for functional ingredients from several previous studies. The addition of non-meat protein (e.g. sodium caseinate and soy protein isolates), hydrocolloids (e. g. konjac flour, carrageenan, and alginates), and MTGase alone or in combination with other functional ingredients improved textural and sensory properties similar to those of regularly processed meats. When MTGase was combined with hydrocolloids (konjac flour or sodium alginate) or other functional ingredients, gelling properties of meat protein were improved even at a low salt level. Based on these reviews, functional ingredients combined with new processing technologies could be incorporated into processed meats to improve the functionality of various low-fat/salt meat products.

• Journal of Microbiology and Biotechnology
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• v.19 no.6
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• pp.588-595
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• 2009

A bacterial strain, YK-2, was isolated as a producer of trans glutaminase from a forest soil sample of Daegu, Korea. The isolate showed a G+C content of 72.7 mol%, contained meso-$A_2pm$ as the cell-wall amino acid, and possessed menaquinone MK-9 ($H_6$) and menaquinone MK-9 ($H_8$) at a ratio of 6:4. The chemotaxonomic analysis, as well as phylogenetic analysis based on the 16S rDNA sequence, identified the isolate as a member of Streptomyces platensis. For transglutaminase production, the optimum medium composition was determined to be 2% glucose, 1% polypeptone, 1% soy tone, and 0.1% $MnCl_2$. The transglutaminase was stable within the pH range of 5.0-9.0 and $30-45^{\circ}C$, and the optimum pH and temperature were pH 8.0 and $45^{\circ}C$, respectively, without any requirement for $Ca^{2+}$.

• Korean Journal of Food Science and Technology
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• v.37 no.2
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• pp.164-170
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• 2005

To improve functional properties of food proteins, homologous or heterologous ${\beta}-casein$ and 11S globulin(glycinin) from animal and vegetable proteins, respectively, were bio-hybridized using transglutaminase(MTGase). Susceptibility was confirmed by SDS-PAGE, particle size analyzed, and emulsion stability tested using Reddy and Fogler method, To determine how bio-hybridized protein influences emulsion stability, protein bound on oil droplet was investigated using Scanning Electron Microscopy (SEM). formation of bio-hybridized protein band was detected among homologous and heterologous proteins, with heterologous protein forming weak band in oligomer form. Homologous ${\beta}-casein$ protein showed high emulsion stability, while homologous glycinin showed almost no stability. Stability of heterologous ${\beta}-casein$ and glycinin protein was higher than that of glycinin. SEM photographs showed even distribution of bio-hybridized proteins on oil droplet improved stability.