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- W2354182334 abstract "A chitinase was isolated from the seeds of mung bean (Phaseolus mungo) by the procedure containing aqueous extraction, affinity chromatography Affi-gel and ion exchange chromatography on SP-Toyopearl. The purified enzyme exhibited a single band on SDS-PAGE with a molecular weight of 30.8?kDa both in reduced and oxidized conditions, indicating it is monomeric protein. The pI was measured to be 6.3 by isoelectric focusing. This enzyme showed its optimum activity at pH?5.4, and a temperature between 40?℃ and 50?℃. These results demonstrated the purified protein was a kind of new chitinase." @default.
- W2354182334 created "2016-06-24" @default.
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- W2354182334 date "2004-01-01" @default.
- W2354182334 modified "2023-09-28" @default.
- W2354182334 title "Purification and enzymatic characterization of a chitinase from Phaseolus mungo" @default.
- W2354182334 hasPublicationYear "2004" @default.
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