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首页> 外文期刊>Catalysis Communications >Immobilization of beta-galactosidase from Kluyveromyces lactis onto a polysiloxane-polyvinyl alcohol magnetic(mPOS-PVA)composite for lactose hydrolysis
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Immobilization of beta-galactosidase from Kluyveromyces lactis onto a polysiloxane-polyvinyl alcohol magnetic(mPOS-PVA)composite for lactose hydrolysis

机译:从Kluyveromyces乳酸固定β-半乳糖苷酶在聚硅氧烷 - 聚乙烯醇磁性(MPOS-PVA)复合材料上,用于乳糖水解

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摘要

beta-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS-PVA,using glutaral-dehyde as activating agent and its properties were evaluated.The enzymatic water insoluble derivative displayed the same optimum pH(6.5)and optimum temperature(50°C)of the soluble enzyme.The apparent K_m~(app)and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different.The mPOS-PVA p-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme.This immobilized p-galactosidase also was effective in hydrolyzing lactose from milk.Hence,one can conclude that mPOS-PVA is an attractive and efficient support for p-galactosidase immobilization.
机译:来自Kluyveromyces乳酸的β-半乳糖苷酶在使用戊二醛-DYHYE作为活化剂中共价固定在MPOS-PVA上,并评估其性质。酶水不溶性衍生物显示相同的最佳pH(6.5)和最佳温度(50℃)和最佳温度(50℃)。 可溶性酶。发现可溶性和固定化酶衍生物的表观K_M〜(APP)和活化能量没有显着差异。MPOS-PVA p-半乳糖苷酶制剂呈现比可溶性酶更高的操作和热稳定性。本 固定化的p-半乳糖苷酶也有效地从牛奶水解乳糖中。可以得出结论,MPOS-PVA是对对P-半乳糖苷酶固定化的有吸引力和有效的支持。

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