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《Periodical of Ocean University of China》 2015-08
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Immobilization of Polyphenol Oxidase and Its Enzymatic Properties

WANG Han;LI Jin;CHENG Hua-Li;MA Qi-Min;College of Environmental Science and Engineering,Ocean University of China;The Key Laboratory of the Marine Environment and Ecology,Ministry of Education,Ocean University of China;  
Polyphenol oxidase(PPO)was immobilized on chitosan/montmorillonite intercalation composites by adsorption and glutaraldehyde cross-linking.The immobilization conditions and enzymatic properties were investigated in detail.Optimal preparation conditions of the immobilization of polyphenol oxidase by adsorption(A-PPO)were pH=5.0,enzyme/support weight ratio 20mg/g,immobilization time 6h.And the protein loading yield of A-PPO was 12.12mg/g,enzyme activity of the unit support 12.76×103U/g,and activity recovery 81.7%.Optimal preparation conditions of enzyme immobilizated by glutaraldehyde cross-linking(C-PPO)were found to be pH=4.0,enzyme/support weight ratio 75mg/g,immobilization time 6h.The protein loading yield of C-PPO was 18.33mg/g,enzyme activity of the unit support2.78×103 U/g,and activity recovery 12.91%.A-PPO and C-PPO showed the optimum activity at pH=8.0,and 40℃and 30℃,respectively.Compared with free PPO,immobilization enhanced enzyme stability against changes in pH and temperature.Immobilized PPO retained more than 37.6% of its initial activity after five cycles.A-PPO and C-PPO had a higher Kmvalues(Michaelis constant)than free enzyme,and the values were 0.56,3.06 and 0.48mmol/L,respectively.The maximum reaction rate Vmaxof A-PPO and C-PPO were decreased compared with free enzyme,and determined as 2.08,0.18 and 2.70U/g,respectively.
【Fund】: 国家自然科学基金项目(41106067);; 山东省自然科学基金项目(ZR2010BQ013);; 青岛市基础研究计划项目(13-1-4-252-jch);; 中国海洋大学中央高校基本科研业务费专项资金项目(201013032)资助
【CateGory Index】: Q814.2
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