ArticleMolecules (Basel, Switzerland)2026
Effect of Storage Duration on Amylase, Protease, and Lipase Activities in Ultrasound-Assisted Extracted Bovine Pancreatin.
Article in Molecules (Basel, Switzerland), 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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Abstract
Long-term stability of multienzyme protein systems is governed by preservation of conformational integrity and resistance to thermally induced structural destabilization. This study evaluated bovine pancreatin (BP) obtained by conventional extraction (CM) and ultrasound-assisted extraction (UAM) during 0-930 days of storage at 10-40 °C. Amylolytic (AA), proteolytic (PA), and lipolytic activities (LA), representing the functional enzymatic activity (EA) of the multienzyme protein system, were monitored to characterize degradation kinetics and activity loss associated with conformational destabilization. After 930 days at 20 ± 1 °C, UAM retained 76% of initial AA compared with 58% for CM, corresponding to a 31% higher residual activity in UAM. LA demonstrated comparatively high stability in both preparations (~84% retention), whereas PA exhibited delayed degradation and significantly higher residual values in UAM samples. Two-way ANOVA confirmed significant effects of extraction method, storage duration, and their interaction (
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