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Transglutaminase from newly isolated Streptomyces sp. CBMAI 1617: Production optimization, characterization and evaluation in wheat protein and dough systems
- Ceresino, Elaine B., de Melo, Ricardo R., Kuktaite, Ramune, Hedenqvist, Mikael S., Zucchi, Tiago D., Johansson, Eva, Sato, Helia H.
- Food chemistry 2018 v.241 pp. 403-410
- Fourier transform infrared spectroscopy, Streptomyces mobaraensis, crosslinking, dough, fermentation, flour, food industry, gliadin, glutenins, polymers, protein-glutamine gamma-glutamyltransferase, response surface methodology, statistical analysis, wheat protein
- The popularity of transglutaminase (TG) by the food industry and the variation in functionality of this enzyme from different origins, prompted us to isolate and evaluate a high-yielding TG strain. Through the statistical approaches, Plackett-Burman and response surface methodology, a low cost fermentation media was obtained to produce 6.074±0.019UmL−1 of TG from a novel source; Streptomyces sp. CBMAI 1617 (SB6). Its potential exploitation was compared to commonly used TG, from Streptomyces mobaraensis. Biochemical and FT-IR studies indicated differences between SB6 and commercial TG (Biobond™ TG-M). Additions of TG to wheat protein and flour based doughs revealed that the dough stretching depended on the wheat protein fraction, TG amount and its origin. A higher degree of cross-linking of glutenins and of inclusion of gliadin in the polymers was seen for SB6 as compared to commercial TG. Thus, our results support the potential of SB6 to tailor wheat protein properties within various food applications.