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immobilization of Candida antarcticaLipase B by Covalent Attachmentto Green Coconut Fiber

机译:通过共价附着于绿色椰子纤维固定念珠菌抗氨基磷酶B.

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The objective of this study was to covalently immobilize Candida antarctica type B lipase (CALB) onto silanized green coconut fibers, Variables known to control the number of bonds between enzyme and support were evaluated including contact time, pH, and final reduction with sodium borohydride. Optimal conditions for lipase immobilization were found to be 2 h incubation at both pH 7.0 and 10.0. Thermal stability studies at 60°C showed that the immobilized lipase prepared at pH 10.0 (CALB-10) was 363-fold more stable than the soluble enzyme and 5.4-fold more stable than the biocatalyst prepared at pH 7.0 (CALB-7). CALB-7 was found to have higher specific activity and better stability when stored at 5°C When sodium borohydride was used as reducing agent on CALB-10 there were no improvement in storage stability and at 60°C stability was reduced for both CALB-7 and CALB-10.
机译:本研究的目的是将Candida抗原型B脂肪酶(CALB)共价固定到硅烷化的绿色椰子纤维上,评价了用硼氢化钠的接触时间,pH和最终减少来评估酶和载体之间键数的变量。 发现脂肪酶固定化的最佳条件在pH 7.0和10.0中孵育2小时。 在60℃下的热稳定性研究表明,在pH10.0(CALB-10)下制备的固定化脂肪酶比可溶性酶更稳定,比在pH7.0(CALB-7)上制备的生物催化剂更稳定5.4倍。 当CALB-10上使用硼氢化钠作为还原剂时储存时,CALB-7具有更高的特异性活性和更好的稳定性,因为CALB-10上还没有改善储存稳定性,并且在60℃下降低了稳定性的稳定性 7和CALB-10。

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