Applied Biochemistry and Biotechnology

, Volume 162, Issue 5, pp 1506–1516

Reduction of Benzaldehyde Catalyzed by Papain-Based Semisynthetic Enzymes

Authors

  • Chun-xiang Chen
    • College of Chemistry, Chemical Engineering and BiotechnologyDonghua University
  • Bo Jiang
    • College of Chemistry, Chemical Engineering and BiotechnologyDonghua University
  • E. A. Carrey
    • Institute of Child HealthLondon’s Global University
    • College of Chemistry, Chemical Engineering and BiotechnologyDonghua University
    • Songjiang University
Article

DOI: 10.1007/s12010-009-8856-9

Cite this article as:
Chen, C., Jiang, B., Carrey, E.A. et al. Appl Biochem Biotechnol (2010) 162: 1506. doi:10.1007/s12010-009-8856-9

Abstract

Some features of native enzyme’s active site were used to conjunction with a chemical reagent or modifying group, which would generate new functionality different from the natural enzyme. In order to obtain an efficient catalyst, we have designed four different molecular size N-derivatives of modifiers and introduced them into the active site of papain to obtain new semisynthetic enzymes, which were used as catalyst in reduction of benzaldehyde to yield benzyl alcohol respectively, and the reactions carried out with recycling agent in 0.1 M phosphate buffer pH 6.5 at 37 °C. The results had shown that a longer N-derivative of semisynthetic enzyme had higher catalytic activity. Furthermore, we propose a plausible model for the catalytic mechanism in the semisynthetic enzymes system.

Keywords

PapainSemisynthetic enzymeReduction

Copyright information

© Humana Press 2010