Substrate specificity of commercial lipases activated by a hydration-aggregation pretreatment in anhydrous esterification reactions.

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  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 8003761 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0909 (Electronic) Linking ISSN: 01410229 NLM ISO Abbreviation: Enzyme Microb Technol Subsets: MEDLINE
    • Publication Information:
      Publication: New York, NY : Elsevier
      Original Publication: [Guildford, Eng.] IPC Science and Technology Press.
    • Subject Terms:
    • Abstract:
      Substrate specificity in non-aqueous esterification catalyzed by commercial lipases activated by hydration-aggregation pretreatment was investigated. Four microbial lipases from Rhizopus japonicus, Burkholderia cepacia, Rhizomucor miehei, and Candida antarctica (fraction B) were used to study the effect of the carbon chain length of saturated fatty acid substrates on the esterification activity with methanol in n-hexane. Hydration-aggregation pretreatment had an activation effect on all lipases used, and different chain length dependencies of esterification activity for lipases from different origins were demonstrated. The effects of various acidic substrates with different degrees of unsaturation, aromatic rings, and alcohol substrates with different carbon chain lengths on esterification activity were examined using R. japonicus lipase, which demonstrated the most remarkable activity enhancement after hydration-aggregation pretreatment. Furthermore, in the esterification of myristic acid with methanol catalyzed by the hydrated-aggregated R. japonicus lipase, maximum reaction rate (5.43 × 10 -5 mmol/(mg-biocat min)) and Michaelis constants for each substrate (48.5 mM for myristic acid, 24.7 mM for methanol) were determined by kinetic analysis based on the two-substrate Michaelis-Menten model.
      Competing Interests: Declaration of Competing Interest This study did not receive any specific grants from funding agencies in the public, commercial, or not-for-profit sectors.
      (Copyright © 2024 Elsevier Inc. All rights reserved.)
    • Contributed Indexing:
      Keywords: Fatty acid methyl ester; Kinetic analysis; Lipase-catalyzed synthesis; Non-aqueous enzymology
    • Accession Number:
      EC 3.1.1.3 (Lipase)
      0 (Fungal Proteins)
      Y4S76JWI15 (Methanol)
      0I3V7S25AW (Myristic Acid)
      059QF0KO0R (Water)
      0 (Bacterial Proteins)
      0 (Fatty Acids)
      0 (Hexanes)
      2DDG612ED8 (n-hexane)
    • Subject Terms:
      Rhizomucor miehei
    • Publication Date:
      Date Created: 20240818 Date Completed: 20240913 Latest Revision: 20240913
    • Publication Date:
      20240914
    • Accession Number:
      10.1016/j.enzmictec.2024.110497
    • Accession Number:
      39154569