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Orientador(es)
Resumo(s)
The modification of anhydrous butterfat via interesterification reactions with oleic acid catalyzed by a lipase from
Mucor circinelloides immobilized by adsorption onto hydrophobic hollow fibers is described. A reasonable
degree of incorporation of free (externally added) oleic acid into the triacylglycerols of butterfat has been
achieved while short-chain fatty acid residues remained virtually unaffected. Total saturated triacylglycerols
decreased by 27%, and triacylglycerols with 32–44 acyl carbons (which contained two or three lauric, myristic,
or palmitic acid residues) decreased by 33%. Total monoene and polyene triacylglycerols increased by 21% and
17%, respectively. The triacylglycerols (TAG) of interesterified butterfat had approximately 27% more oleic acid
residues and approximately 8% less lauric, 6% less myristic, and 6% less palmitic acid residues than those of
the original butterfat; the fraction of low-melting TAG peak increased by 19% whereas that of high-melting TAG
decreased by 83%. Although a certain degree of butterfat hydrolysis was observed, enzymatic acidolysis was
technically feasible and able to produce a modified butterfat with a stronger nutraceutical character.
Descrição
Palavras-chave
Interesterification Immobilized lipase Butterfat Hollow-fiber bioreactor Mucor circinelloides
Contexto Educativo
Citação
BALCÃO, Victor M. ...[et al] - Lipase-catalyzed acidolysis of butterfat with oleic acid: characterization of process and product. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 23 (1998), p. 118–128
Editora
Elsevier