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Comparative studies on enzymatic changes and structure of lipases under ultrasound.

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  • Additional Information
    • Source:
      Publisher: Springer Country of Publication: Germany NLM ID: 101565857 Publication Model: Print-Electronic Cited Medium: Print ISSN: 2190-572X (Print) Linking ISSN: 21905738 NLM ISO Abbreviation: 3 Biotech Subsets: PubMed not MEDLINE
    • Publication Information:
      Original Publication: Berlin : Springer
    • Abstract:
      The influences of ultrasound pretreatment on the catalytic activity, enzymatic properties and structure of two commercial lipases, Novozym51032 (lipase N) and Palatase20000L (lipase P), were studied by comparing the lipase kinetic and thermodynamic parameters of lipase and protein structure analysis. The experimental results showed that lipase N showed enhanced activity, while lipase P showed reduced activity under identical ultrasound conditions. Furthermore, the V max of lipase N increased and the free energy (ΔG) decreased, whereas lipase P showed the opposite change. Both lipases underwent hydrophobic group exposure, yet the changes in their secondary structures were in opposition to one another. The intermolecular aggregates of lipase N were fragmented into small aggregates by ultrasound, a phenomenon not observed with lipase P. This result demonstrates that ultrasound stimulation enhances lipase activity primarily through the modulation of enzyme secondary structure and the disruption of intermolecular aggregates. Moreover, ultrasound treatment has been demonstrated to enhance the storage stability of the enzyme. These results demonstrate the potential value of ultrasound treatment in optimizing enzymes and bioprocesses.
      Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-025-04310-9.
      (© King Abdulaziz City for Science and Technology 2025. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.)
    • Abstract:
      Conflict of interestThe authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
    • Contributed Indexing:
      Keywords: Catalytic activity; Enzymatic properties; Storage stability; Structure; Ultrasound
    • Publication Date:
      Date Created: 20250505 Latest Revision: 20250708
    • Publication Date:
      20260130
    • Accession Number:
      PMC12048379
    • Accession Number:
      10.1007/s13205-025-04310-9
    • Accession Number:
      40321715