Immobilization of lipase on chitin and its use in nonconventional blocatalysis

被引：79

作者：

Gomes, FM ^{[1
]}

Pereira, EB ^{[1
]}

de Castro, HF ^{[1
]}

机构：

[1] Fac Engn Quim Lorena, Dept Chem Engn, Biocatalysis Lab, BR-12606970 Lorena, SP, Brazil

来源：

BIOMACROMOLECULES | 2004年 / 5卷 / 01期

关键词：

D O I：

10.1021/bm0342077

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chitin was funcionalized with hexamethylenediamine followed by glutaraldehyde activation, and its capacity to bind Candida rugosa lipase was investigated. The loading of 250 units g(-1) support showed to be effective, resulting in a uniform enzyme fixation with high catalytic activity. Both free and immobilized lipases were characterized by determining the activity profile as a function of pH, temperature, and thermal stability. For the immobilized lipase, the influence of the reaction temperature and substrate polarity in nonconventional biocatalysis was also analyzed. Production of butyl esters was found to be dependent on the substrate partition coefficient, which accounts the greatest value for the system butanol and butyric acid. The highest enzyme activity was found for the system butanol and caprylic acid at a reaction temperature of 40degreesC. Under such conditions, the operational stability tests indicated that a small enzyme deactivation occurs after 12 batches, revealing a biocatalyst half-life of 426.7 h.

引用

页码：17 / 23

页数：7

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