Volume 5, Issue 19 (7-2015)
NCMBJ 2015, 5(19): 24-31 |
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Khesali Aghtaei H, Sattari S, Vahabzadeh F. Immobilization of Rhizopus oryzae on loofa sponge affects interacellularly produced lipases. NCMBJ 2015; 5 (19) :24-31
URL: http://ncmbjpiau.ir/article-1-658-en.html
URL: http://ncmbjpiau.ir/article-1-658-en.html
Faculty of Chemical Engineering Amirkabir University , Far@aut.ac.ir
Abstract: (7298 Views)
Aim and background: lipase is a carboxylic ester hydrolase enzyme (EC.3.1.1.3), which acts on triglycerides to release fatty acids, monoglycerides, diglycerides and glycerol. With respect to the biological process advantages against chemical process plus the ability of lipase to catalyze the revers reaction (i.e., esterification) a vast chapter on this enzyme scientific applications was started. The focusing point in this study was to determine the optimum cultivation time for free and immobilized form of Rhizopus oryzae with regard to producing membrane-bound lipase. With the usage of n-butanol and oleic acid in a non-polar environment (n-hexane as solvent) the esterification reaction was carried out while the effect of molecular sieves on the final yield was considered.
Materials and methods: Rhizopus oryzae cells in the form of immobilized on cellulose support particles or free cells are used as a whole cell bicatalyst. Colorimetric method was used for measuring the esterification activity (i.e., determination of residual free fatty acid in reaction media).
Results: Membrane-bound lipasees which are produced by both, immobilized and free form of the cell reach their maximum activity after 48 hour. Also the biocatalyst esterification activity was improved approximately 4-folds by the immobilization of fungal cell on loofa sponge. More than 96% efficiency was gained in synthesis of 1-butyl-oleate ester in the presence of 4 g molecular sieve.
Conclusion: Immobilization could improve the membrane-bound lipase esterification activity. The lipase secretion to the culture media significantly affected by cultivation time. To reach a complete esterification reaction (approximately 100%), water adsorption with use of molecular sieve is an appropriate method.
Materials and methods: Rhizopus oryzae cells in the form of immobilized on cellulose support particles or free cells are used as a whole cell bicatalyst. Colorimetric method was used for measuring the esterification activity (i.e., determination of residual free fatty acid in reaction media).
Results: Membrane-bound lipasees which are produced by both, immobilized and free form of the cell reach their maximum activity after 48 hour. Also the biocatalyst esterification activity was improved approximately 4-folds by the immobilization of fungal cell on loofa sponge. More than 96% efficiency was gained in synthesis of 1-butyl-oleate ester in the presence of 4 g molecular sieve.
Conclusion: Immobilization could improve the membrane-bound lipase esterification activity. The lipase secretion to the culture media significantly affected by cultivation time. To reach a complete esterification reaction (approximately 100%), water adsorption with use of molecular sieve is an appropriate method.
Type of Study: Research Article |
Subject:
Cellular and molecular
Received: 2015/07/16 | Accepted: 2015/07/16 | Published: 2015/07/16
Received: 2015/07/16 | Accepted: 2015/07/16 | Published: 2015/07/16
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