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<p>This study investigates how microwave irradiation influences the catalytic activity, kinetic behavior, and conformational properties of papain and α-amylase. Progressive increases in microwave power (200–800&#xa0;W) and treatment time (3–12&#xa0;min) resulted in a reduction of catalytic activity for both enzymes. Detailed kinetic analysis revealed variations in residual activity, <i>Vmax</i>, <i>Km</i>, <i>kcat</i>, <i>kcat/Km</i> values under different power and treatment time. The observed reduction in free sulfhydryl content, along with alterations in UV absorption spectra, intrinsic fluorescence, surface hydrophobicity, indicated conformational changes in both enzymes, likely due to disruption of inter- and intramolecular interactions. A decline in α-helix, β-sheets, and turns while increasing random coils of microwave-treated α-amylase, whereas a decline in α-helix, turns, and random coil while increasing β-sheets in microwave-treated papain, reflecting the secondary structural rearrangements. Furthermore, enhanced peak intensities in the infrared spectra of both enzymes suggested modifications in their primary structures. An alteration in particle size and ζ-potential denoted unfolding and partial denaturation of papain and α-amylase. Collectively, these findings demonstrate that microwave irradiation induces structural alterations at different power inputs and treatment, adversely affecting the catalytic efficiency of papain and α-amylase.</p>

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Assessing the Impact of Microwave Irradiation on Papain and α-amylase

  • 期刊论文

  • 发表日期：

    2026年5月30日

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  • Jayashree B. Potkule,
  • Manoj Kumar,
  • Uday S. Annapure

摘要

This study investigates how microwave irradiation influences the catalytic activity, kinetic behavior, and conformational properties of papain and α-amylase. Progressive increases in microwave power (200–800 W) and treatment time (3–12 min) resulted in a reduction of catalytic activity for both enzymes. Detailed kinetic analysis revealed variations in residual activity, Vmax, Km, kcat, kcat/Km values under different power and treatment time. The observed reduction in free sulfhydryl content, along with alterations in UV absorption spectra, intrinsic fluorescence, surface hydrophobicity, indicated conformational changes in both enzymes, likely due to disruption of inter- and intramolecular interactions. A decline in α-helix, β-sheets, and turns while increasing random coils of microwave-treated α-amylase, whereas a decline in α-helix, turns, and random coil while increasing β-sheets in microwave-treated papain, reflecting the secondary structural rearrangements. Furthermore, enhanced peak intensities in the infrared spectra of both enzymes suggested modifications in their primary structures. An alteration in particle size and ζ-potential denoted unfolding and partial denaturation of papain and α-amylase. Collectively, these findings demonstrate that microwave irradiation induces structural alterations at different power inputs and treatment, adversely affecting the catalytic efficiency of papain and α-amylase.