ArticleFood chemistry: X2026
Adsorption-crosslinking immobilization of SHSL on NKA macroporous resin: Operational stability and molecular dynamics at the enzyme-resin interface.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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12 authors.
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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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