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<p>Proteases are vital industrial enzymes, contributing approximately 60% of the global enzyme market, by facilitating protein hydrolysis. Fruit peels, a major agricultural waste, offer a sustainable alternative for commercial enzyme production. This study investigates the proteases extracted from the peels of <i>Punica granatum</i>, <i>Musa acuminata</i>, <i>Carica papaya</i>, and <i>Ananas comosus</i>, with a primary focus on determining their optimal pH, temperature, and substrate specificity. Additionally, <i>Kₘ</i> and <i>Vₘₐₓ</i> kinetics were assessed to characterize their catalytic efficiency. Optimal proteolytic activity was observed at pH 8 and 30&#xa0;°C for <i>P. granatum</i>, pH 7 and 30&#xa0;°C for <i>M. acuminata</i>, pH 8 and 30&#xa0;°C for <i>C. papaya</i>, and pH 7 and 50&#xa0;°C for <i>A. comosus</i>. substrate specificity of protease was assessed using casein, fish meal, soybean meal, black soldier fly larvae, bovine serum albumin, and egg albumin, revealing broad applicability, especially in <i>P. granatum</i> peels. The stability of <i>P. granatum</i> proteases across substrates suggests multiple isoforms or a flexible active site. Kinetic analysis using Lineweaver-Burk plots revealed Vmax and K<sub>M</sub> values of 8.45 µmol/min/mL and 3.81 µM (<i>P. granatum</i>), 4.56 µmol/min/mL and 10.08 µM (<i>M. acuminata</i>), 2.98 µmol/min/mL and 2.84 µM (<i>C. papaya</i>), and 2.97 µmol/min/mL and 11.38 µM (<i>A. comosus</i>) respectively. Among the tested fruit peels, <i>P. granatum</i> exhibited the highest reaction rate, while <i>C. papaya</i> demonstrated the highest substrate affinity, making them as promising candidates for feed supplementation and industrial enzyme applications. The broad substrate specificity and high catalytic efficiency of <i>P. granatum</i> further reinforce its potential for use in feed formulations, enhancing protein hydrolysis and improving nutrient availability. These findings highlight the significant potential of fruit peel-derived proteases in promoting sustainable enzyme production and advancing bioeconomic applications.</p>

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Kinetic characterisation of proteases from Punica granatum, Musa acuminata, Carica papaya, and Ananas comosus as sustainable enzyme sources

  • 期刊论文

  • 发表日期：

    2026年1月3日

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  • Jhanani Gopalraaj,
  • Krishnakumar Velayudhannair

摘要

Proteases are vital industrial enzymes, contributing approximately 60% of the global enzyme market, by facilitating protein hydrolysis. Fruit peels, a major agricultural waste, offer a sustainable alternative for commercial enzyme production. This study investigates the proteases extracted from the peels of Punica granatum, Musa acuminata, Carica papaya, and Ananas comosus, with a primary focus on determining their optimal pH, temperature, and substrate specificity. Additionally, Kₘ and Vₘₐₓ kinetics were assessed to characterize their catalytic efficiency. Optimal proteolytic activity was observed at pH 8 and 30 °C for P. granatum, pH 7 and 30 °C for M. acuminata, pH 8 and 30 °C for C. papaya, and pH 7 and 50 °C for A. comosus. substrate specificity of protease was assessed using casein, fish meal, soybean meal, black soldier fly larvae, bovine serum albumin, and egg albumin, revealing broad applicability, especially in P. granatum peels. The stability of P. granatum proteases across substrates suggests multiple isoforms or a flexible active site. Kinetic analysis using Lineweaver-Burk plots revealed Vmax and KM values of 8.45 µmol/min/mL and 3.81 µM (P. granatum), 4.56 µmol/min/mL and 10.08 µM (M. acuminata), 2.98 µmol/min/mL and 2.84 µM (C. papaya), and 2.97 µmol/min/mL and 11.38 µM (A. comosus) respectively. Among the tested fruit peels, P. granatum exhibited the highest reaction rate, while C. papaya demonstrated the highest substrate affinity, making them as promising candidates for feed supplementation and industrial enzyme applications. The broad substrate specificity and high catalytic efficiency of P. granatum further reinforce its potential for use in feed formulations, enhancing protein hydrolysis and improving nutrient availability. These findings highlight the significant potential of fruit peel-derived proteases in promoting sustainable enzyme production and advancing bioeconomic applications.