In this workα-amylase was immobilized on magnetic Fe3O4 nanoparticles with polyethylenimine(PEI)/polydopamine(PDA)coating or 3-aminopropyl triethoxysilane(APTES)for the first time via adsorption–precipitation–cross...In this workα-amylase was immobilized on magnetic Fe3O4 nanoparticles with polyethylenimine(PEI)/polydopamine(PDA)coating or 3-aminopropyl triethoxysilane(APTES)for the first time via adsorption–precipitation–cross-linking.Compared with the freeα-amylase,the resultant magnetic cross-linkedα-amylase aggregates(PEI/PDA-M-CLEAs and N-M-CLEAs)exhibited excellent thermal and storage stability as well as pH stability.After storage at 25°C for 60 days,freeα-amylase only retained 60%of its initial activity,while PEI/PDA-M-CLEAs and N-M-CLEAs retained 80%and 78%of their initial activities,respectively.Furthermore,N-M-CLEAs and PEI/PDA-M-CLEAs showed good reusability.After 6 repeated uses,PEI/PDA-M-CLEAs and N-M-CLEAs still maintained 65%and 62%of their initial activities,respectively.Especially,PEI/PDA-M-CLEAs and N-M-CLEAs exhibited higher starch hydrolysis efficiency than freeα-amylase.The maximum dextrose equivalent(DE)values of starch hydrolysis by PEI/PDA-M-CLEAs and N-M-CLEAs reached 29.24%and 28.79%within 90 min,respectively.However,the maximum DE values of starch hydrolysis by the freeα-amylase was only 27.89%even in 150 min.The magnetic cross-linkedα-amylase aggregates could be introduced as effective biocatalyst for industrial applications in production of maltose syrups.展开更多
基金the Fundamental Research Funds for the Central Universities(grant No.226-2023-0085)the Science and Technology Program of Tianjin,China(grant No.20ZYJDJC00080)the International Collaboration Project(grant No.2020/37/K/ST8/03805).
文摘In this workα-amylase was immobilized on magnetic Fe3O4 nanoparticles with polyethylenimine(PEI)/polydopamine(PDA)coating or 3-aminopropyl triethoxysilane(APTES)for the first time via adsorption–precipitation–cross-linking.Compared with the freeα-amylase,the resultant magnetic cross-linkedα-amylase aggregates(PEI/PDA-M-CLEAs and N-M-CLEAs)exhibited excellent thermal and storage stability as well as pH stability.After storage at 25°C for 60 days,freeα-amylase only retained 60%of its initial activity,while PEI/PDA-M-CLEAs and N-M-CLEAs retained 80%and 78%of their initial activities,respectively.Furthermore,N-M-CLEAs and PEI/PDA-M-CLEAs showed good reusability.After 6 repeated uses,PEI/PDA-M-CLEAs and N-M-CLEAs still maintained 65%and 62%of their initial activities,respectively.Especially,PEI/PDA-M-CLEAs and N-M-CLEAs exhibited higher starch hydrolysis efficiency than freeα-amylase.The maximum dextrose equivalent(DE)values of starch hydrolysis by PEI/PDA-M-CLEAs and N-M-CLEAs reached 29.24%and 28.79%within 90 min,respectively.However,the maximum DE values of starch hydrolysis by the freeα-amylase was only 27.89%even in 150 min.The magnetic cross-linkedα-amylase aggregates could be introduced as effective biocatalyst for industrial applications in production of maltose syrups.
