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- Lim, Lihui; Senba, Hironori; Kimura, Yukihiro; Yokota, Satoko; Doi, Mikiharu; Yoshida, Ken-Ichi; Takenaka, Shinji
- Process biochemistry 2019 v.79 pp. 74-80
- thermal stability; Komagataella pastoris; decolorization; polyacrylamide gel electrophoresis; industry; molecular weight; Aspergillus glaucus; sequence analysis; meat; mutagenesis; tuna; water content; hydrolysis; aspartic proteinases; detergents; meat processing; glycosylation; hemoglobin; pH; mutants; heme proteins; water activity
- ... Aspergillus glaucus MA0196 produces a highly glycosylated aspartic protease (PepA_MA0196) that shows hydrolytic and decolorization activities toward hemoglobin. Sequence analysis of PepA_MA0196 indicated two potential N-glycosylation consensus sites, at Asn131 and Asn275. To elucidate the role of N-glycosylation in the biochemical properties of PepA_MA0196 and the resulting effects, recombinant Pe ...
- Liang, Youxiang; Jiao, Song; Wang, Miaomiao; Yu, Huimin; Shen, Zhongyao
- Process biochemistry 2019 v.79 pp. 49-56
- Agrobacterium radiobacter; Escherichia coli; Rhodococcus ruber; biocatalysts; enantiomers; epichlorohydrins; epoxide hydrolase; epoxides; glycols; pH; proteins; thermal stability
- ... Epoxide hydrolases (EHs) are attractive enzymes for producing enantiopure epoxides and diols, but do not display enough stability when lysates or Escherichia coli whole cells are used as biocatalysts. In this work, an organic-solvent tolerant strain Rhodococcus ruber THdAdN was utilized to overexpress an epoxide hydrolase from Agrobacterium radiobacter (ArEH), using E. coli BL21(DE3) as a control. ...