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An unusual reversible sol-gel transition phenomenon in organogels and itsapplication for enzyme immobilization in gelatin membranes

机译:有机凝胶中异常的可逆溶胶-凝胶转变现象及其在明胶膜固定化酶中的应用

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摘要

An unusual phenomenon is observed for gelatin solutions (1.7-6.8%) in the microemulsion system of 0.3 M bis(2-ethylhexyl)sulfosuccinate sodium salt in isooctane and 14.5% distilled water. Highly viscous gels obtained at temperatures above 30 degrees C become free-flowing liquids at low temperatures (5-10 degrees C). This reversible temperature-dependent sol-gel transition phenomenon is used to immobilize several enzymes, such as lipase from Candida rugosa, alcohol dehydrogenase from baker's yeast, mandelonitrile lyase from Sorghum bicolor, and horseradish peroxidase in the gelatin matrix by solubilizing the enzyme in a microemulsion-based gelatin solution at low temperature (<5 degrees C) and then cross-linking with glutaraldehyde. The enzymes retain 70-80% of their activity after immobilization and can be used in biotransformations in organic solvents without any changes in enantioselectivity. This work provides a unique low-temperature technique for enzyme immobilization in a biocompatible gelatin matrix with a great flexibility of size and shape.
机译:在异辛烷和14.5%蒸馏水中的0.3 M双(2-乙基己基)磺基琥珀酸钠盐的微乳液体系中,明胶溶液(1.7-6.8%)观察到不寻常的现象。在高于30摄氏度的温度下获得的高粘度凝胶在低温(5-10摄氏度)下变为自由流动的液体。这种可逆的依赖温度的溶胶-凝胶转变现象可用于固定几种酶,例如将微乳化酶将其固定在明胶基质中,例如固定来自假丝酵母的脂肪酶,来自面包酵母的酒精脱氢酶,来自高粱双色的扁桃腈裂解酶和辣根过氧化物酶。基低温明胶溶液(<5摄氏度),然后与戊二醛交联。固定后,酶保留其活性的70-80%,可用于有机溶剂的生物转化,而对映选择性没有任何变化。这项工作为将酶固定在生物相容性明胶基质中提供了独特的低温技术,具有很大的尺寸和形状灵活性。

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