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<p>This study explores the surface display of <i>Lactobacillus paracasei</i> aspartate ammonia-lyase (LpAAL) on <i>Pichia pastoris</i> using glycosylphosphatidylinositol (GPI) anchoring technology. LpAAL, an enzyme with broad substrate specificity, has significant potential in various industries, including food, pharmaceuticals, and cosmetics, due to its ability to catalyze the conversion of L-aspartate into fumarate and other related reactions. The surface-displayed LpAAL on yeast (yLpAAL) demonstrated improved stability, especially under high temperature and alkaline conditions, making it suitable for industrial processes that demand robust and stable enzymes. Kinetic analysis revealed a slight increase in <i>K</i><sub>m</sub> value (6.3&#xa0;mM) for yLpAAL comparing to free LpAAL (5.9&#xa0;mM), reflecting reduced substrate affinity, but without a notable impact on overall efficiency. Additionally, yLpAAL exhibited enhanced storage stability and reusability, maintaining over 85% of its activity after six consecutive cycles. We successfully demonstrate the surface display technology to enhance enzyme performance by yLpAAL, offering a promising strategy for industries requiring durable and efficient enzymes in challenging environments.</p>

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Surface display of aspartate ammonia-lyase from Lactobacillus paracasei on Pichia pastoris

  • 期刊论文

  • 发表日期：

    2025年4月15日

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  • Chen-Chi Chang,
  • Yi-Hao Huang,
  • Hua-Kun Fu,
  • Kai-Wei Chang,
  • Shih-Hsuan Chen,
  • Yu-Ting Yu,
  • Xin-Ying Lau,
  • Jhih-Ying Ciou,
  • He-Yuan Hsieh,
  • Yung-Ju Chen,
  • Lu-Sheng Hsieh

摘要

This study explores the surface display of Lactobacillus paracasei aspartate ammonia-lyase (LpAAL) on Pichia pastoris using glycosylphosphatidylinositol (GPI) anchoring technology. LpAAL, an enzyme with broad substrate specificity, has significant potential in various industries, including food, pharmaceuticals, and cosmetics, due to its ability to catalyze the conversion of L-aspartate into fumarate and other related reactions. The surface-displayed LpAAL on yeast (yLpAAL) demonstrated improved stability, especially under high temperature and alkaline conditions, making it suitable for industrial processes that demand robust and stable enzymes. Kinetic analysis revealed a slight increase in Km value (6.3 mM) for yLpAAL comparing to free LpAAL (5.9 mM), reflecting reduced substrate affinity, but without a notable impact on overall efficiency. Additionally, yLpAAL exhibited enhanced storage stability and reusability, maintaining over 85% of its activity after six consecutive cycles. We successfully demonstrate the surface display technology to enhance enzyme performance by yLpAAL, offering a promising strategy for industries requiring durable and efficient enzymes in challenging environments.