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<p>To enhance catalytic performance of porcine pancreas lipase, it was immobilized on wheat bran powder as a carrier using physical adsorption between enzyme protein and bran cellulose in a column glass bottle. In the transesterification of n-hexanol and vinyl acetate for 8&#xa0;h at 37℃ and 160&#xa0;rpm, the immobilized lipase behaved desired activity when the mass ratio of enzyme to wheat bran was 10 : 30 (mg : mg), being a 12.8-fold increase compared to 10&#xa0;mg of native lipase. By approximate estimation, the loading capacity and immobilization yields of this immobilized lipase were 313.3&#xa0;mg/g and 94%, respectively. In the transesterification, the expressed activity of this immobilized lipase, relative to native lipase, was 1443%, based on the initial conversion within the first 4&#xa0;h. And the immobilized lipase converted hexanol exceeded 96% at 37℃ and 160&#xa0;rpm after 48&#xa0;h, whereas the native lipase achieved only 13%. Even after five cycles of 8-hour reactions, the immobilized enzyme retained an activity converting 10% of substrate, while the native lipase maintained only 0.3% substrate conversion capability. In the hydrolysis of soybean oil and peanut oil, the immobilized lipase exhibited hydrolysis rates approximately 1.9-fold and 3.8-fold those of the native lipase, respectively. These results demonstrate that wheat bran as a carrier can significantly enhance the transesterification and hydrolysis activities of this lipase, indicating its great potential for applications such as a nonaqueous catalyst or a feed additive to improve fat digestion in animals.</p> Graphical Abstract <p></p>

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Improved Catalysis of Porcine Pancreas Lipase Adsorbed on Wheat Bran

  • 期刊论文

  • 发表日期：

    2026年6月30日

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  • Yingchao Wang,
  • Lu Chen,
  • Fangdi Cong,
  • Liyao Liu,
  • Wei Yang,
  • Chang Li,
  • Xinyang Gao,
  • Huiyi Jin,
  • Yanling Xu,
  • Zhaowang Shen

摘要

To enhance catalytic performance of porcine pancreas lipase, it was immobilized on wheat bran powder as a carrier using physical adsorption between enzyme protein and bran cellulose in a column glass bottle. In the transesterification of n-hexanol and vinyl acetate for 8 h at 37℃ and 160 rpm, the immobilized lipase behaved desired activity when the mass ratio of enzyme to wheat bran was 10 : 30 (mg : mg), being a 12.8-fold increase compared to 10 mg of native lipase. By approximate estimation, the loading capacity and immobilization yields of this immobilized lipase were 313.3 mg/g and 94%, respectively. In the transesterification, the expressed activity of this immobilized lipase, relative to native lipase, was 1443%, based on the initial conversion within the first 4 h. And the immobilized lipase converted hexanol exceeded 96% at 37℃ and 160 rpm after 48 h, whereas the native lipase achieved only 13%. Even after five cycles of 8-hour reactions, the immobilized enzyme retained an activity converting 10% of substrate, while the native lipase maintained only 0.3% substrate conversion capability. In the hydrolysis of soybean oil and peanut oil, the immobilized lipase exhibited hydrolysis rates approximately 1.9-fold and 3.8-fold those of the native lipase, respectively. These results demonstrate that wheat bran as a carrier can significantly enhance the transesterification and hydrolysis activities of this lipase, indicating its great potential for applications such as a nonaqueous catalyst or a feed additive to improve fat digestion in animals.

Graphical Abstract