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- W2354328223 abstract "Aeromonas caviae CB101 can secrete multiple chitinases into the culture supernatant as revealed by chitinase activity staining.One gene chi1 has been cloned and sequenced.It encodes a protein of 865 amino acids with a signal peptide at the N-terminal,of which a polycystic-kidney-disease(PKD)-like domain,a triosephosphate-isomerase(TIM) catalytic region,a receptor-for egg jelly(REJ)-like domain and two chitin-binding-domain(chBDs) locate from the N-terminal to C-terminal.A chitinase was isolated from the culture and purified by the steps of ammonium sulfate precipitation,DEAE-Sepharose and Mono Q anion exchange column chromatography.The result of it's N-terminal sequencing approves that it is the truncation of the signal peptide and some C-terminal domains of the cloned chitinase Chi1.When spray the CB101's cosmid library on the plates containing the antibiotic and 1% colloid chitin,nine clones that can utilize chitin were gotten and were proved to be chitinase.The isolation and purification of chitinase following N-terminal sequencing and other experiments suggest that the Aeromonas caviae CB101 can only secrete one chitinase,which are Chi1 and its truncates." @default.
- W2354328223 created "2016-06-24" @default.
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- W2354328223 date "2007-01-01" @default.
- W2354328223 modified "2023-09-23" @default.
- W2354328223 title "Purification,characterization and gene clone of Chitinase from Aeromonas caviae CB101" @default.
- W2354328223 hasPublicationYear "2007" @default.
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