期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 56, 期 1, 页码 41-45出版社
ELSEVIER
DOI: 10.1016/j.molcatb.2008.04.002
关键词
Chloroperoxidase; Cross-linked enzyme aggregate; Biocatalysis; Azaindole
A cross-linked enzyme aggregate (CLEA (R)) of chloroperoxidase (CPO) was created that exhibited greatly improved stability in the presence of hydrogen peroxide concentrations as high as 1.2 M, The CPO-CLEA was generated by oxidizing the protein with sodium periodate and precipitating and cross-linking with ammonium sulfate and Sodium borohydride. CLEA (R) production parameters, including the concentrations of these three reagents, were optimized to maximize the activity of the biocatalyst in oxidizing 7-azaindole to 7-azaoxindole. Additionally, the in situ production of the CLEA (R) was demonstrated. resulting in a process for converting >90% of 5 g/17-azaindole in <1 h while requiring neither gradual pet-oxide addition nor immobilized enzyme isolation. (C) 2008 Elsevier B.V. All rights reserved.
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