Effects of pH and NaCl on hydrolysis and transpeptidation activities of a salt-tolerant γ-glutamyltranspeptidase from Bacillus amyloliquefaciens S0904
| Autor: | Jae-Ick Lee, Young-Wan Kim, Hye-Bin Cho, Hyeon-Gyu Yang, Wu-Jin Park, Jun-Ho Ahn |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Bacillus amyloliquefaciens biology γ glutamyltranspeptidase Wild type Salt (chemistry) 04 agricultural and veterinary sciences biology.organism_classification 040401 food science 01 natural sciences Applied Microbiology and Biotechnology law.invention Hydrolysis 0404 agricultural biotechnology Enzyme chemistry Biochemistry law 010608 biotechnology Recombinant DNA Specific activity Food Science Biotechnology |
| Zdroj: | Food Science and Biotechnology. 30:853-860 |
| ISSN: | 2092-6456 1226-7708 |
| DOI: | 10.1007/s10068-021-00928-6 |
| Popis: | Bacillus amyloliquefaciens S0904 was selected as a hyperproducer of a glutamine-hydrolyzing enzyme which was identified as a γ-glutamyltranspeptidase catalyzing both hydrolysis and transpeptidation of glutamyl substrates. The signal peptide-truncated recombinant enzyme (rBAGGT) showed two-fold enhanced specific activity for hydrolysis and optimum pH shift to pH 7 from pH 6 compared with the wild type. The hydrolysis activity of 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 the hydrolysis activity but also inhibited the transpeptidation activity to be ignorable. By contrast, at pH 9 in the absence of NaCl, the alkaline pH-favored transpeptidation activity was 99% of the maximum with only 15% of the maximum hydrolysis activity. In conclusion, the hydrolysis and transpeptidation activities of the recombinant BAGGT is controllable by changing pH and whether or not to add NaCl. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink