Effects of pH and NaCl on hydrolysis and transpeptidation activities of a salt-tolerant γ-glutamyltranspeptidase from Bacillus amyloliquefaciens S0904
Effects of pH and NaCl on hydrolysis and transpeptidation activities of a salt-tolerant γ-glutamyltranspeptidase from Bacillus amyloliquefaciens S0904
- 주제(키워드) y-Glutamyltranspeptidase , Glutamine hydrolysis , Transpeptidation , Salt tolerance , pH dependency
- 발행기관 한국식품과학회
- 발행년도 2021
- 총서유형 Journal
- DOI http://dx.doi.org/10.1007/s10068-021-00928-6
- KCI ID ART002725328
- 본문언어 영어
초록/요약
Bacillus amyloliquefaciens S0904 was selectedas a hyperproducer of a glutamine-hydrolyzing enzymewhich was identified as a c-glutamyltranspeptidase catalyzingboth hydrolysis and transpeptidation of glutamylsubstrates. The signal peptide-truncated recombinantenzyme (rBAGGT) showed two-fold enhanced specificactivity for hydrolysis and optimum pH shift to pH 7 frompH 6 compared with the wild type. The hydrolysis activityof rBAGGT was tolerant against NaCl up to 2.5 M,whereas the transpeptidation activity decreased by NaCl. At pH 6, the addition of 1.5 M NaCl not only enhanced thehydrolysis activity but also inhibited the transpeptidationactivity to be ignorable. By contrast, at pH 9 in the absenceof NaCl, the alkaline pH-favored transpeptidation activitywas 99% of the maximum with only 15% of the maximumhydrolysis activity. In conclusion, the hydrolysis andtranspeptidation activities of the recombinant BAGGT iscontrollable by changing pH and whether or not to addNaCl.
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