Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases

The enzymatic transesterification of palm olein was conducted in a low-moisture medium with nonspecific and 1,3-specific lipases from microbial sources. The enzymes were first immobilized on Celite, lyophilized for 4 h and then added to a reaction medium that consisted of 10% (wt/vol) palm olein in...

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Main Authors: Ghazali, H.M., Hamidah, S., Che Man, Y.B.
Format: Article
Published: AOCS Press 1995
Online Access:http://psasir.upm.edu.my/id/eprint/114351/
https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02635647
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spelling my.upm.eprints.1143512025-01-14T06:56:07Z http://psasir.upm.edu.my/id/eprint/114351/ Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases Ghazali, H.M. Hamidah, S. Che Man, Y.B. The enzymatic transesterification of palm olein was conducted in a low-moisture medium with nonspecific and 1,3-specific lipases from microbial sources. The enzymes were first immobilized on Celite, lyophilized for 4 h and then added to a reaction medium that consisted of 10% (wt/vol) palm olein in water-saturated hexane. The catalytic performance of the enzymes was evaluated by determining the changes in triglyceride (TG) composition and concentrations by reverse-phase high-performance liquid chromatography (HPLC) and the formation of free fatty acids by titration. Studies with lipase from Candida rugosa showed that the degree of hydrolysis was reduced by drying the immobilized preparation and that the best drying time was 4 h. In all cases, the transesterification process resulted in the formation of PPP, a TG initially undetected in the oil, and increases in the concentrations of OOO (1.3–2.1-fold), OOL (1.7–4.5-fold), and OLL (1.7–4.3-fold), where P, O, and L are palmitic, oleic, and linoleic acids, respectively. SOS (where S is stearic acid), another TG not detected in the oil, was synthesized by Rhizomucor miehei and Pseudomonas lipases, with the latter producing more of this TG. There was a corresponding decrease in the concentrations of POP, PLP, POO, and POL. PPP concentration ranged from 1.9% (w/w) for Mucor javanicus lipase to 6.2% (w/w) for Pseudomonas lipase after 24 h. The greatest degree and fastest rate of change were caused by Pseudomonas lipase, followed by the enzymes from R. miehei and Aspergillus niger. The effects of transesterification and hydrolysis of palm olein by the various lipases resulted in changes in the overall degree of saturation of the triglyceride components. There seems to be no clear correlation between the enzyme positional specificity and the products formed. Possible mechanisms for the formation of PPP, OOL, OLL, OOO, and SOS are discussed. AOCS Press 1995 Article PeerReviewed Ghazali, H.M. and Hamidah, S. and Che Man, Y.B. (1995) Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases. Journal of the American Oil Chemists’ Society, 72 (6). pp. 633-639. ISSN 0003-021X; eISSN: 1558-9331 https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02635647 10.1007/BF02635647
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description The enzymatic transesterification of palm olein was conducted in a low-moisture medium with nonspecific and 1,3-specific lipases from microbial sources. The enzymes were first immobilized on Celite, lyophilized for 4 h and then added to a reaction medium that consisted of 10% (wt/vol) palm olein in water-saturated hexane. The catalytic performance of the enzymes was evaluated by determining the changes in triglyceride (TG) composition and concentrations by reverse-phase high-performance liquid chromatography (HPLC) and the formation of free fatty acids by titration. Studies with lipase from Candida rugosa showed that the degree of hydrolysis was reduced by drying the immobilized preparation and that the best drying time was 4 h. In all cases, the transesterification process resulted in the formation of PPP, a TG initially undetected in the oil, and increases in the concentrations of OOO (1.3–2.1-fold), OOL (1.7–4.5-fold), and OLL (1.7–4.3-fold), where P, O, and L are palmitic, oleic, and linoleic acids, respectively. SOS (where S is stearic acid), another TG not detected in the oil, was synthesized by Rhizomucor miehei and Pseudomonas lipases, with the latter producing more of this TG. There was a corresponding decrease in the concentrations of POP, PLP, POO, and POL. PPP concentration ranged from 1.9% (w/w) for Mucor javanicus lipase to 6.2% (w/w) for Pseudomonas lipase after 24 h. The greatest degree and fastest rate of change were caused by Pseudomonas lipase, followed by the enzymes from R. miehei and Aspergillus niger. The effects of transesterification and hydrolysis of palm olein by the various lipases resulted in changes in the overall degree of saturation of the triglyceride components. There seems to be no clear correlation between the enzyme positional specificity and the products formed. Possible mechanisms for the formation of PPP, OOL, OLL, OOO, and SOS are discussed.
format Article
author Ghazali, H.M.
Hamidah, S.
Che Man, Y.B.
spellingShingle Ghazali, H.M.
Hamidah, S.
Che Man, Y.B.
Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
author_facet Ghazali, H.M.
Hamidah, S.
Che Man, Y.B.
author_sort Ghazali, H.M.
title Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
title_short Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
title_full Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
title_fullStr Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
title_full_unstemmed Enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
title_sort enzymatic transesterification of palm olein with nonspecific and 1,3-specific lipases
publisher AOCS Press
publishDate 1995
url http://psasir.upm.edu.my/id/eprint/114351/
https://aocs.onlinelibrary.wiley.com/doi/10.1007/BF02635647
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score 13.239859