Microwave-assisted rapid characterization of lipase selectivities.

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  • Author(s): Bradoo S;Bradoo S; Rathi P; Saxena RK; Gupta R
  • Source:
    Journal of biochemical and biophysical methods [J Biochem Biophys Methods] 2002 Apr 18; Vol. 51 (2), pp. 115-20.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier/North-Holland Biomedical Press Country of Publication: Netherlands NLM ID: 7907378 Publication Model: Print Cited Medium: Print ISSN: 0165-022X (Print) Linking ISSN: 0165022X NLM ISO Abbreviation: J Biochem Biophys Methods Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam, Elsevier/North-Holland Biomedical Press.
    • Subject Terms:
      Microwaves*; Bacteria/*enzymology ; Biochemistry/*methods ; Lipase/*chemistry; Animals ; Ascorbic Acid/chemistry ; Hydrogen-Ion Concentration ; Hydrolysis ; Lipase/metabolism ; Substrate Specificity ; Sucrose/chemistry ; Swine ; Time Factors ; Triglycerides/chemistry
    • Abstract:
      A rapid screening procedure for characterization of lipase selectivities using microwaves was developed. The rate of reaction of various commercial lipases (porcine pancreas, Mucor miehei, Candida rugosa, Pseudomonas cepacia) as well as lipases from laboratory isolates-Bacillus stearothermophilus and Burkholderia cepacia RGP-10 for triolein hydrolysis was 7- to 12-fold higher in a microwave oven as compared to that by pH stat. The esterification of sucrose/methanol and ascorbic acid with different fatty acids was also achieved within 30 s in a microwave using porcine pancreas, B. stearothermophilus SB-1 and B. cepacia RGP-10 lipases. The relative rates and selectivity of the lipases both for hydrolytic and synthesis reactions remains unaltered. However, the rate of reaction was dynamically enhanced when exposed to microwaves. Microwave-assisted enzyme catalysis can become an attractive procedure for rapid characterization of large number of enzyme samples and substrates, which otherwise is a cumbersome and time-consuming exercise.
    • Accession Number:
      0 (Triglycerides)
      57-50-1 (Sucrose)
      EC 3.1.1.3 (Lipase)
      PQ6CK8PD0R (Ascorbic Acid)
    • Publication Date:
      Date Created: 20020614 Date Completed: 20020719 Latest Revision: 20190916
    • Publication Date:
      20221213
    • Accession Number:
      10.1016/s0165-022x(02)00005-2
    • Accession Number:
      12062110