Báo cáo khoa học: Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS
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The enzymatic properties of chitinase A fromVibrio carchariaehave been studied in detail by using combined HPLC and electrospray MS. This approach allowed the separation ofaandbanomers and the simultaneous monitoring of chitooligosaccharide products down to picomole levels. Chi-tinase A primarily generated b-anomeric products, indicating that it cata-lyzed hydrolysis through a retaining mechanism.
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