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- W2108859892 abstract "ABSTRACT A new microbial transglutaminase (MTGase or MTG, EC 2.3.2.13) from a Streptomyces sp. strain isolated from Brazilian soil samples was purified and characterized. Enzyme purification was fast and simple, consisting of two successive chromatographies on Sephadex G-75 columns with yields of 48 and 17%, respectively. The protein purification was successfully achieved to electrophoretical homogeneity on sodium dodecyl sulphate–polyacrylamide gel electrophoresis. The molecular mass of the MTGase was estimated to be about 45 kDa. The enzyme exhibited optimal activity in the pH range of 6.0–6.5 and at 35–40C. It was stable over a broad pH range (4.5–8.0) and up to 45C. The purified MTG's activity was independent of Ca+2, but was activated by the presence of K+, Ba2+, Na+, and Co2+, and inhibited by Cu2+ and Hg2+, which suggests a thiol group at its active site. The purified enzyme presented a Km of 6.37 mM and a Vmax of 1.7 U/mL. PRACTICAL APPLICATION Transglutaminase-catalyzed reactions can be used to modify the functional properties of food proteins. Transglutaminase has been used to catalyze the cross-linking of a number of proteins, such as whey proteins, soy proteins, gluten, myosin and actomyosin. The modification of food proteins by transglutaminase may lead to textured products, help to protect lysine residues in food proteins from various chemical reactions, encapsulate lipids and/or lipid-soluble materials, form heat- and water-resistant films, avoid heat treatment in gelation processes, improve elasticity and water holding capacity, modify solubility and functional properties and produce food proteins of higher nutritional value through the cross-linking of different proteins containing complementary limiting essential amino acids. Due all its potentials, the search for new biotechnological sources of transglutaminase and the study of new enzymes characteristics are essential for the reduction of the enzyme costs and development of new applications for the food industry." @default.
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- W2108859892 date "2011-08-01" @default.
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- W2108859892 title "PURIFICATION AND CHARACTERIZATION OF A NEW TRANSGLUTAMINASE FROM STREPTOMYCES SP. ISOLATED IN BRAZILIAN SOIL" @default.
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- W2108859892 doi "https://doi.org/10.1111/j.1745-4514.2010.00456.x" @default.
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