• 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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.6
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• pp.801-806
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• 2009

A species producing transglutaminase (EC 2.3.2.13) was isolated from forest soil and identified as Streptomyces platensis YK-2. The transglutaminase was purified from culture broth by 50% methanol precipitation, followed by successive chromatography on DEAE-Sephadex. The yield and purification-fold was 63.4% and 2.2-fold, respectively. The purified microbial transglutaminase (MTG) migrated as a single band of approximately 45 kDa upon sodium dodecyl sulfate polyacrylamide gel eletrophoresis. The isoelectric point determined by multichambered electrofocusing was pH $6.0{\sim}7.0$. The enzyme was strongly inhibited by $Hg^{++}$, but was activated by $Cd^{++}$, $Mg^{++}$, $Mn^{++}$, $Pb^{++}$ and reducing agents such as dithiothreitol and mercaptoethanol.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.782-790
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• 2011

The effects of soy protein isolate (SPI) and red bean protein isolate (RBPI) on gelling properties of pork myofibrillar protein (MP) in the presence of microbial transglutaminase (MTG) were studied at 0.45 M NaCl. MP paste was incubated with MTG (0.1%) at various levels (0.1, 0.3, 0.5, and 1%) of SPI and RBPI before incubating at $4^{\circ}C$ for 4 h. The rheological property results showed that MP gel shear stress increased with increasing RBPI concentration. Cooking yield (CY) of the MP gel increased with increasing RBPI and SPI, whereas gel strength (GS) was not affected by adding RBPI or SPI. Thus, effects of incubation time (0, 4, 8, 10, and 12 h) were measured at 0.1% SPI and RBPI. GS values of the MP gel at 10 and 12 h were similar and were higher than those of the others. CY values were highest when RBPI (0.1%) was added, regardless of incubation time. The protein patterns indicated that incubating the MP with MTG for 10 h resulted in protein crosslinking between MP and RBPI or SPI. Based on these results, RBPI and SPI could be used as an ingredient to increase textural properties and cooking yield of meat protein gel.

• Macromolecular Research
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• v.15 no.7
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• pp.671-675
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• 2007

Soybean proteins appear to harbor a great deal of potential as functional ingredients due to the fact that they are composed of highly bioavailable peptides and amino acids. To develop drink- or gel-type foods formulated with soybean protein, the physicochemical properties of intact and chemically modified soy glycinin were assessed. Maleylation to soy glycinin altered the surface charges of glycinin via the modification of lysine residues, and subsequently generated the dissociation of glycinin subunits owing to the increase in charge repulsion. This modification thus improved the solubility of glycinin, particularly under acidic pH conditions. It is worthy of note that maleylation increased the susceptibility of the basic subunits of mTGase and the formation of a substantial quantity of molecules at a low protein solution concentration. The results of dynamic rheological studies indicated that the 5% intact glycinin progressively formed the gel with mTGase treatment in a concentration-dependent manner, but maleylated-glycinin did not.