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Peer-reviewedCC BY-NC-NDFood chemistry: X

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

  • Wei Wu1,2
  • Yunzhu Chen2,3
  • Peiwang Li2
  • Jiali Ren1,3
  • Wenyan Yuan1
  • Yan Yang2,3
  • Zhihong Xiao2
  • Xiao Zhou2,3
  • Yan Chao2
  • Shengyu Guo4
  • Jingzhen Chen2
  • Changzhu Li1,2,5
5 affiliations
  1. 1State Key Laboratory of Woody Oil Resources Utilization, Faculty of Food Science and Engineering, Central South University of Forestry and Technology, 498 South Shaoshan Road, Changsha, Hunan 410004, PR China.
  2. 2Hunan Academy of Forestry, Changsha, Hunan 410004, PR China.
  3. 3Yuelushan Laboratory, Changsha, Hunan 410000, PR China.
  4. 4Department of economics and management, ChangSha University, Changsha, Hunan 410022, PR China.
  5. 5Institute of Urban Agriculture, Chinese Academy of Agricultural Sciences, Chengdu, Sichuan 610213, PR China.
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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.

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Cite

BibTeXRIS
BibTeX
@article{wu2026adsorptioncrosslinking,
  title = {{Adsorption-crosslinking immobilization of SHSL on NKA macroporous resin: Operational stability and molecular dynamics at the enzyme-resin interface.}},
  author = {Wei Wu and Yunzhu Chen and Peiwang Li and Jiali Ren and Wenyan Yuan and Yan Yang and Zhihong Xiao and Xiao Zhou and Yan Chao and Shengyu Guo and Jingzhen Chen and Changzhu Li},
  journal = {Food chemistry: X},
  year = {2026},
  month = oct,
  doi = {10.1016/j.fochx.2026.104598},
  url = {https://europepmc.org/article/MED/42908790},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Adsorption-crosslinking immobilization of SHSL on NKA macroporous resin: Operational stability and molecular dynamics at the enzyme-resin interface.
AU  - Wei Wu
AU  - Yunzhu Chen
AU  - Peiwang Li
AU  - Jiali Ren
AU  - Wenyan Yuan
AU  - Yan Yang
AU  - Zhihong Xiao
AU  - Xiao Zhou
AU  - Yan Chao
AU  - Shengyu Guo
AU  - Jingzhen Chen
AU  - Changzhu Li
PY  - 2026
DA  - 2026/10/07
JO  - Food chemistry: X
DO  - 10.1016/j.fochx.2026.104598
UR  - https://europepmc.org/article/MED/42908790
AB  - 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.
SN  - 2590-1575
ER  -