Chem. J. Chinese Universities ›› 2010, Vol. 31 ›› Issue (9): 1774.

• Articles • Previous Articles     Next Articles

Preparation and Properties of Cross-linked Enzyme Aggregates of Papain

WANG Meng-Fan, QI Wei*, SU Rong-Xin, HE Zhi-Min   

  1. State Key Laboratory of Chemical Engineering(Tianjin University), Chemical Engineering Research Center, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China
  • Received:2009-12-14 Online:2010-09-10 Published:2010-09-10
  • Contact: QI Wei. E-mail: qiwei@tju.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 20976125)、国家“八六三”计划项目(批准号: 2008AA10Z318)、教育部新世纪优秀人才(批准号: NCET-08-0386)、教育部科学技术研究重点项目(批准号: 108031)和天津市应用基础研究计划项目(批准号: 10JCYBJC05100)资助.

Abstract: Cross-linked enzyme aggregates(CLEAs) is a non-carrier immobilization technique with the advantages of simple preparation, low cost and high unit activity. In this paper, papain-CLEAs were prepared and the effects of precipitation and cross-linking on CLEAs activity were investigated. It is shown that the highest activity of papain-CLEAs were obtained when using pure ethanol as precipitant, 40% glutaraldehyde as cross-linker and cross-linking at 4 ℃ for 16 h. Moreover, the optimal catalytic conditions and operational stabilities of papain-CLEAs were characterized. Papain-CLEAs shifted the optimal pH from 7.0 to 6.0 and broaden the optimal temperature to the range of 50—80 ℃. Papain-CLEAs also enhanced thermal and storage stabilities compared with free enzyme. It is indicated from the morphology that these improved performances resulted from the high surface area and multi-points covalent cross-linking structure of every single papain-CLEAs. These improved characters show practical advantages of papain-CLEAs in biocatalysis.

Key words: Cross-linked enzyme aggregate, Immobilization, Papain, Stability, Morphology, Cluster

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