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<p>To enhance the nonaqueous catalysis of lipases, <i>Pseudomonas cepacia</i> lipase was immobilized on cotton fibers dyed with tetra-<i>β</i>-amino-phthalocyanine zinc or tetra-<i>β</i>-nitro-phthalocyanine zinc by physical adsorption in a column glass bottle and used to catalyze transesterification between hexanol and vinyl acetate. The suitable ratios of lipase to immobilized carriers were 10: 10 (mg: mg), and the employed carriers enhanced the enzymatic activity by more than 2.3-fold during the initial reaction stage. When the immobilized lipases were subjected to repeated uses at 37&#xa0;°C and 160&#xa0;rpm, their nonaqueous stability followed this order: cotton dyed with tetra-<i>β</i>-amino-phthalocyanine zinc &gt; cotton fibers &gt; cotton dyed with tetra-<i>β</i>-nitro-phthalocyanine zinc. The decrease in their substrate conversion efficiency after 24&#xa0;h was 5.7%, 24.7%, and 33.3%, respectively, indicating that tetra-<i>β</i>-amino-phthalocyanine zinc provides effective protection for the enzyme.&#xa0;</p>

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Enhanced Nonaqueous Stability of Pseudomonas Cepacia Lipase Immobilized on Phthalocyanine-Dyed Absorbent Cotton

  • 期刊论文

  • 发表日期：

    2025年6月19日

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  • Yingchao Wang,
  • Xing Zhao,
  • Fangdi Cong,
  • Wei Yang,
  • Liyao Liu,
  • Zhaowang Shen

摘要

To enhance the nonaqueous catalysis of lipases, Pseudomonas cepacia lipase was immobilized on cotton fibers dyed with tetra-β-amino-phthalocyanine zinc or tetra-β-nitro-phthalocyanine zinc by physical adsorption in a column glass bottle and used to catalyze transesterification between hexanol and vinyl acetate. The suitable ratios of lipase to immobilized carriers were 10: 10 (mg: mg), and the employed carriers enhanced the enzymatic activity by more than 2.3-fold during the initial reaction stage. When the immobilized lipases were subjected to repeated uses at 37 °C and 160 rpm, their nonaqueous stability followed this order: cotton dyed with tetra-β-amino-phthalocyanine zinc > cotton fibers > cotton dyed with tetra-β-nitro-phthalocyanine zinc. The decrease in their substrate conversion efficiency after 24 h was 5.7%, 24.7%, and 33.3%, respectively, indicating that tetra-β-amino-phthalocyanine zinc provides effective protection for the enzyme.