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Applied Biochemistry and Biotechnology

, Volume 76, Issue 3, pp 183–191 | Cite as

Preparation and properties of immobilized pig kidney aminoa cylase and optical resolution of N-acyl-dl-alanine

  • Hao-Jing Wang
  • Ji-Hong Bai
  • De-Shan Liu
  • Tong Zhang
  • Hai-Meng ZhouEmail author
Article

Abstract

Aminoacylase (EC 3.5.1.14) was immobilized into DEAE-Sephadex A-25 by ion-exchange absorption for optical resolution of N-acyl-dl-alanine. The effects of pH, temperature, and Co2+ concentration on the activity of free and immobilized enzymes were in vestigated along with the operational and the thermal stability of the immobilized enzyme. The immobilized enzyme retained high catalytic activity. The optimum pH and temperature for the hydrolysis of N-acyl-l-alanine in the dl-isomer mixture were 8.0 and 65°C, respectively. Co2+ was an activator for the immobilized enzyme in a similarroleas for the free enzyme. Nosignificant loss of activity was observed for at least 300 h of continuous operation. The yield of l-alanine was about 70% of the theoretical yield. The immobilized aminoacylase column decayed over a very long period of operation, but could be completely reactivated by regeneration.

Index Entries

Aminoacylase pig kidney immobilization optical resolution 

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Copyright information

© Humana Press Inc 1999

Authors and Affiliations

  • Hao-Jing Wang
    • 1
    • 2
  • Ji-Hong Bai
    • 1
  • De-Shan Liu
    • 2
  • Tong Zhang
    • 1
  • Hai-Meng Zhou
    • 1
    Email author
  1. 1.Department of Biological Science and BiotechnologyTsinghua UniversityBeijingChina
  2. 2.Department of Chemical EngineeringTsinghua UniversityBeijingChina

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