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

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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.

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Authors and Affiliations

  1. Department of Biological Science and Biotechnology, Tsinghua University, 100084, Beijing, China

    Hao-Jing Wang, Ji-Hong Bai, Tong Zhang & Hai-Meng Zhou

  2. Department of Chemical Engineering, Tsinghua University, 100084, Beijing, China

    Hao-Jing Wang & De-Shan Liu

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  1. Hao-Jing Wang
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  2. Ji-Hong Bai
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  3. De-Shan Liu
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  4. Tong Zhang
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  5. Hai-Meng Zhou
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Correspondence to Hai-Meng Zhou.

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Wang, HJ., Bai, JH., Liu, DS. et al. Preparation and properties of immobilized pig kidney aminoa cylase and optical resolution of N-acyl-dl-alanine. Appl Biochem Biotechnol 76, 183–191 (1999). https://doi.org/10.1385/ABAB:76:3:183

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  • DOI: https://doi.org/10.1385/ABAB:76:3:183

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