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酶水凝胶膜的催化活性和长期稳定性对固化时间的依赖性。

Dependence of catalytic activity and long-term stability of enzyme hydrogel films on curing time.

机构信息

Department of Chemistry, University of Canterbury, Christchurch, New Zealand.

出版信息

Bioelectrochemistry. 2010 Aug;79(1):142-6. doi: 10.1016/j.bioelechem.2009.12.004. Epub 2010 Jan 6.

DOI:10.1016/j.bioelechem.2009.12.004
PMID:20051328
Abstract

Enzyme hydrogels were prepared on carbon film electrodes using glucose oxidase and an epoxide crosslinking agent. The catalytic activity of the gels was found to depend strongly on curing time. The competing effects of increased mechanical stability and decreased enzyme activity as curing time increases resulted in the highest catalytic activity for films cured for 24h at 25 degrees C. Weekly electrochemical measurements established that the long-term stabilities of all hydrogels cured for 24-72 h were similar, with close to half of the initial catalytic activity being retained after immersion for 3 months in agitated phosphate buffer solution at 25 degrees C.

摘要

酶水凝胶是使用葡萄糖氧化酶和环氧化物交联剂在碳膜电极上制备的。发现凝胶的催化活性强烈依赖于固化时间。随着固化时间的增加,机械稳定性的提高和酶活性的降低之间的竞争效应导致在 25°C 下固化 24 小时的薄膜具有最高的催化活性。每周进行电化学测量,结果表明,所有固化 24-72 小时的水凝胶的长期稳定性相似,在 25°C 的搅拌磷酸盐缓冲溶液中浸泡 3 个月后,保留了近初始催化活性的一半。

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