首页> 外文期刊>Journal of the Indian Institute of Science >PARTIAL PURIFICATION AND SOME PROPERTIES OF A POLYGALACTURONASE PRODUCED EXTRACELLULARLY BY Alternaria alternata (FR.) KEISSL.
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PARTIAL PURIFICATION AND SOME PROPERTIES OF A POLYGALACTURONASE PRODUCED EXTRACELLULARLY BY Alternaria alternata (FR.) KEISSL.

机译:交链孢霉(Alterneraria alternata)(FR。)KEISSL胞外生产的半乳糖醛酸酶的部分纯化和某些性质。

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摘要

A polygalacturonase was purified to about 480 fold from the culture filtrate of Alternaria alternata (Fr.) Keissl. The partially purified enzyme had a pH optimum of 5.2 and activation energy of 4.77K cal/mole for polygalacturonic acid (sodium salt). Vmax,
机译:从Alternaria alternata(Fr.)Keissl的培养滤液中纯化出半乳糖醛酸酶至约480倍。对于多半乳糖醛酸(钠盐),部分纯化的酶的最适pH为5.2,活化能为4.77K cal / mol。最大功率

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