Gelation of Food Protein Induced by Recombinant Microbial Transglutaminase

• Published in: Journal of food science 2003-01, Vol.68 (1), p.48-51
• Main Authors: Yokoyama, K, Ohtsuka, T, Kuraishi, C, Ono, K, Kita, Y, Arakawa, T, Ejima, D
• Format: Article
• Language: English
• Subjects: alpha-casein; Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; Comparative analysis; cross-linking; dietary protein; enzyme activity; Enzymes; Escherichia coli; Fish and seafood industries; Food industries; Food science; Fundamental and applied biological sciences. Psychology; gelation; gelation activity; polyacrylamide gel electrophoresis; Protein folding; protein-glutamine gamma-glutamyltransferase; recombinant; refolding; sodium caseinate; Streptomyces mobaraensis; Streptoverticillium mobaraense; thermal stability; transglutaminase
• ISSN: 0022-1147; 1750-3841
• DOI: 10.1111/j.1365-2621.2003.tb14112.x

The recombinant microbial transglutaminase from Streptoverticillium mobaraense var. (rMTGase) was expressed in Escherichia coli. Specific enzyme activity of rMTGase was comparable to native MTGase. However, the gelation of a sodium caseinate solution induced by rMTGase was slower than that induced by native MTGase. In addition, the mechanical property of kamaboko prepared with rMTGase was weaker than that with native MTGase. In SDS-PAGE analysis, α-casein monomers decreased more slowly during the incubation with rMTGase than MTGase. These results confirmed the difference of cross-linking activity between the 2 enzymes. Furthermore, thermal stability of rMTGase was lower compared to native MTGase. These results suggest that the difference of cross-linking activity and thermal stability between the 2 enzymes cause differences in gelation activity of protein.