Authors: Yuran Zhang Yu Xin Hailin Yang Ling Zhang Xiaole Xia Yanjun Tong Yi Chen Wu Wang
Publish Date: 2013/09/01
Volume: 37, Issue: 4, Pages: 719-725
Abstract
The mechanism of thermal inactivation about xanthine oxidase XOD from Arthrobacter M3 was investigated Results of reducing SDSPAGE indicated that the inactivation of XOD was not related to the peptide degradation Meanwhile fluorimetry and circular dichroism spectroscopy suggested that XOD inactivation might be associated with the exposure of hydrophobic residues to surface and partial loss of secondary structure Specific formation of soluble aggregates of XOD was detected by size exclusion chromatography In addition the thermaldynamic analysis showed that the inactivation kinetics of XOD followed the firstorder model Therefore trehalose cosolute and betaine osmolyte were accordingly employed to attenuate the inactivation of this enzyme The results associated with these two reagents further confirmed that the loss of XOD activity was mainly due to the exposure of hydrophobic residues and formation of aggregation Owing to the added trehalose and betaine halflife could be significantly increased and the inactivation rate constant k was detected as decreasedThis work was supported by Project supported by the National Natural Science Foundation of China Grant No21306064 Natural Science Foundation of Jiangsu Province BK2012119 Program of the Science and Technology Support Plan of Jiangsu Province No BE2010625 and BE2011625 Doctor Candidate Foundation of Jiangnan University JUDCF11012 the Program of Innovation Projects Plan of Jiangsu Province No CXLX11 0502 the Priority Academic Program Development of Jiangsu Higher Education Institutions111 Project No 111206
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