<p>Enzyme immobilization offers a promising strategy to enhance biocatalyst stability, reusability, and operational performance in industrial bioprocesses. In this study, hydrated silica (HS) was surface-engineered via four distinct chemistries—amination (AHS), carboxylation (CHS), polydopamine coating (DHS), and epoxidation (EHS)—to develop robust carriers for Flavourzyme immobilization. The modified supports were characterized by diffuse reflectance Fourier-transform infrared spectroscopy (DR-FTIR) and X-ray photoelectron spectroscopy (XPS), confirming successful functionalization. Immobilization conditions were optimized for each system through single-factor experiments. Among the carriers, DHS achieved the best overall performance with 42.02% immobilization rate and 73.69% enzyme activity recovery. Compared to free Flavourzyme, immobilized systems demonstrated enhanced pH and thermal stability, broader operational ranges, and superior reusability. DHS-F retained over 50% activity after 20 cycles and exhibited excellent storage stability. Principal component analysis (PCA) identified storage stability and reusability as the key discriminators among immobilized systems. These findings demonstrate that surface-engineered HS, especially DHS, provides a scalable and recyclable platform for stable Flavourzyme immobilization, with potential for continuous operation in food protein hydrolysis processes, supporting sustainable and resource-efficient biocatalytic processes.</p>

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Surface-Engineered Hydrated Silica as a Reusable Support for Flavourzyme Immobilization in Food Protein Hydrolysis

  • Xu Zhao,
  • Yuqin Cheng,
  • Lei Cai,
  • Chun Cui

摘要

Enzyme immobilization offers a promising strategy to enhance biocatalyst stability, reusability, and operational performance in industrial bioprocesses. In this study, hydrated silica (HS) was surface-engineered via four distinct chemistries—amination (AHS), carboxylation (CHS), polydopamine coating (DHS), and epoxidation (EHS)—to develop robust carriers for Flavourzyme immobilization. The modified supports were characterized by diffuse reflectance Fourier-transform infrared spectroscopy (DR-FTIR) and X-ray photoelectron spectroscopy (XPS), confirming successful functionalization. Immobilization conditions were optimized for each system through single-factor experiments. Among the carriers, DHS achieved the best overall performance with 42.02% immobilization rate and 73.69% enzyme activity recovery. Compared to free Flavourzyme, immobilized systems demonstrated enhanced pH and thermal stability, broader operational ranges, and superior reusability. DHS-F retained over 50% activity after 20 cycles and exhibited excellent storage stability. Principal component analysis (PCA) identified storage stability and reusability as the key discriminators among immobilized systems. These findings demonstrate that surface-engineered HS, especially DHS, provides a scalable and recyclable platform for stable Flavourzyme immobilization, with potential for continuous operation in food protein hydrolysis processes, supporting sustainable and resource-efficient biocatalytic processes.