Adsorption-crosslinking immobilization of SHSL on NKA macroporous resin: Operational stability and molecular dynamics at the enzyme-resin interface.

Authors

Wei Wu, Yunzhu Chen, Peiwang Li, Jiali Ren, Wenyan Yuan, Yan Yang, Zhihong Xiao, Xiao Zhou, Yan Chao, Shengyu Guo, Jingzhen Chen, Changzhu Li

Published in

Food chemistry: X. Volume 39. Pages 104598. Epub Oct 07, 2026.

Abstract

Lipase immobilization can improve operational stability, while enzyme-support interactions may alter conformational behavior near the catalytic region. How local support association relates to catalytic-region dynamics remains unclear. Here, SHSL was immobilized on NKA macroporous resin by hydrophobic adsorption followed by glutaraldehyde post-treatment. The optimized preparation showed 91.44 ± 2.39 U/g activity, 65.47% immobilization yield, and 26.2% activity recovery, retaining 53.7% activity after 10 reuse cycles and 61.0% after 35 days of storage versus 11.7% for free SHSL. Glutaraldehyde post-treatment reduced cumulative protein leakage after 10 cycles from 40.14% to 15.38% relative to adsorption alone. In 150-ns molecular dynamics simulations, a representative SHSL-NKA fragment complex maintained persistent noncovalent association away from the catalytic triad. During 50-150 ns, interfacial fluctuations decreased by 31.7%, whereas lid mobility increased by 17.6%. NKA-fragment association also increased lid opening, decreased pocket volume, altered catalytic-residue geometry, and redistributed access-channel occurrence.

PMID:
42908790
Bibliographic data and abstract were imported from PubMed on 23 Oct 2026.

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