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- W2361103629 abstract "To obtain high pure chitinase C from constructed recombinant E.coli pET-22b-chiC,we decreased culture temperature to increase soluble expression of Serratia marcescens chitinase C.The expressed product was purified to electrophoretic homogeneity by immobilized metal ion affinity chromatography(IMAC)and Phenyl-Sepharose hydrophobic interaction chromatography(HIC).The enzyme properties research indicated that the purified chitinase C was a monomeric protein with a molecular weight of 51.8 ku.The optimum pH was 5.0 and the optimum temperature was 55 ℃.And its activity still kept above 90% after 1 h at 55 ℃.Results also showed that the activity of chitinase was significantly inhibited by Cu2+,Hg2+,Co2+,Mg2+,while promoted by Fe2+,Zn2+,Sn2+,Ba2+ and also significantly promoted by Mn2+." @default.
- W2361103629 created "2016-06-24" @default.
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- W2361103629 date "2010-01-01" @default.
- W2361103629 modified "2023-09-23" @default.
- W2361103629 title "Purification and Enzyme Properties of Recombinant Serratia marcescens Chitinase C" @default.
- W2361103629 hasPublicationYear "2010" @default.
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