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Updated: Oct 24, 2026
Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
Adsorption-crosslinking immobilization of SHSL on NKA macroporous resin: Operational stability and molecular dynamics
Wei Wu1,2, Yunzhu Chen2,3, Peiwang Li2
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.
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.
