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<p>Chitin, the second most abundant biomaterial after cellulose, has attracted attention because of its biocompatibility and environmental friendliness, making it suitable for biomedical applications. This study explores the use of chitin monoliths, which are fabricated via thermally induced phase separation (TIPS), for protein separation in a flow system. The chitin monoliths were prepared by modifying chitin into butyryl chitin (BC) and hydrolyzing it to restore its properties. The monoliths were characterized using various techniques, including FE–SEM, ATR FT–IR, and mercury intrusion porosimetry, which revealed pore structures that were tunable on the basis of the quenching temperature. The monoliths exhibited permeability in a flow system and affinity for lysozyme. The monolith efficiently separated lysozyme from ovalbumin in the flow system, and it was able to separate a mixture of artificial sample and diluted hen egg white. The system’s stability was shown through numerous adsorption/desorption cycles, indicating very effective recovery with negligible capacity loss. This flow system was not prone to leakage and was properly dispersed, representing an improvement over a previous system. This study highlights the potential of chitin monoliths as efficient and sustainable tools for protein separation in continuous flow systems, offering improvements over traditional batch methods.</p>

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Protein separation using a chitin monolith with a continuous flow system

  • 期刊论文

  • 发表日期：

    2026年1月22日

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  • Armeida D. R. Madjid,
  • Hikaru Matsumoto,
  • Yoshinori Kawabe,
  • Masanori Nagao,
  • Yoshiko Miura

摘要

Chitin, the second most abundant biomaterial after cellulose, has attracted attention because of its biocompatibility and environmental friendliness, making it suitable for biomedical applications. This study explores the use of chitin monoliths, which are fabricated via thermally induced phase separation (TIPS), for protein separation in a flow system. The chitin monoliths were prepared by modifying chitin into butyryl chitin (BC) and hydrolyzing it to restore its properties. The monoliths were characterized using various techniques, including FE–SEM, ATR FT–IR, and mercury intrusion porosimetry, which revealed pore structures that were tunable on the basis of the quenching temperature. The monoliths exhibited permeability in a flow system and affinity for lysozyme. The monolith efficiently separated lysozyme from ovalbumin in the flow system, and it was able to separate a mixture of artificial sample and diluted hen egg white. The system’s stability was shown through numerous adsorption/desorption cycles, indicating very effective recovery with negligible capacity loss. This flow system was not prone to leakage and was properly dispersed, representing an improvement over a previous system. This study highlights the potential of chitin monoliths as efficient and sustainable tools for protein separation in continuous flow systems, offering improvements over traditional batch methods.