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Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae

Most substrate for esterification has the inherent problem of low miscibility which requires addition of solvents into the reaction media. In this contribution, we would like to present an alternative and feasible option for an efficient solvent-free synthesis of menthyl butyrate using a novel therm...

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Autores principales: Wahab, Roswanira Abdul, Basri, Mahiran, Rahman, Raja Noor Zaliha Raja Abdul, Salleh, Abu Bakar, Rahman, Mohd Basyaruddin Abdul, Chaibakhsh, Naz, Leow, Thean Chor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686904/
https://www.ncbi.nlm.nih.gov/pubmed/26740782
http://dx.doi.org/10.1080/13102818.2014.978220
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author Wahab, Roswanira Abdul
Basri, Mahiran
Rahman, Raja Noor Zaliha Raja Abdul
Salleh, Abu Bakar
Rahman, Mohd Basyaruddin Abdul
Chaibakhsh, Naz
Leow, Thean Chor
author_facet Wahab, Roswanira Abdul
Basri, Mahiran
Rahman, Raja Noor Zaliha Raja Abdul
Salleh, Abu Bakar
Rahman, Mohd Basyaruddin Abdul
Chaibakhsh, Naz
Leow, Thean Chor
author_sort Wahab, Roswanira Abdul
collection PubMed
description Most substrate for esterification has the inherent problem of low miscibility which requires addition of solvents into the reaction media. In this contribution, we would like to present an alternative and feasible option for an efficient solvent-free synthesis of menthyl butyrate using a novel thermostable crude T1 lipase. We investigated the effects of incubation time, temperature, enzyme loading and substrate molar ratio and determined the optimum conditions. The high conversion of menthyl butyrate catalyzed by crude T1 lipase in a solvent-free system is greatly affected by temperature and time of the reaction media. The highest yield of menthyl butyrate was 99.3% under optimized conditions of 60 °C, incubation time of 13.15 h, 2.53 mg, 0.43% (w/w) enzyme to substrate ratio and at molar ratio of butyric anhydride/menthol 2.7:1. Hence, the investigation revealed that the thermostable crude T1 lipase successfully catalyzed the high-yield production of menthyl butyrate in a solvent-free system. The finding suggests that the crude T1 lipase was a promising alternative to overcome shortcomings associated with solvent-assisted enzymatic reactions.
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spelling pubmed-46869042016-01-04 Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae Wahab, Roswanira Abdul Basri, Mahiran Rahman, Raja Noor Zaliha Raja Abdul Salleh, Abu Bakar Rahman, Mohd Basyaruddin Abdul Chaibakhsh, Naz Leow, Thean Chor Biotechnol Biotechnol Equip Article; Food Biotechnology Most substrate for esterification has the inherent problem of low miscibility which requires addition of solvents into the reaction media. In this contribution, we would like to present an alternative and feasible option for an efficient solvent-free synthesis of menthyl butyrate using a novel thermostable crude T1 lipase. We investigated the effects of incubation time, temperature, enzyme loading and substrate molar ratio and determined the optimum conditions. The high conversion of menthyl butyrate catalyzed by crude T1 lipase in a solvent-free system is greatly affected by temperature and time of the reaction media. The highest yield of menthyl butyrate was 99.3% under optimized conditions of 60 °C, incubation time of 13.15 h, 2.53 mg, 0.43% (w/w) enzyme to substrate ratio and at molar ratio of butyric anhydride/menthol 2.7:1. Hence, the investigation revealed that the thermostable crude T1 lipase successfully catalyzed the high-yield production of menthyl butyrate in a solvent-free system. The finding suggests that the crude T1 lipase was a promising alternative to overcome shortcomings associated with solvent-assisted enzymatic reactions. Taylor & Francis 2014-11-02 2014-11-14 /pmc/articles/PMC4686904/ /pubmed/26740782 http://dx.doi.org/10.1080/13102818.2014.978220 Text en © 2014 The Author(s). Published by Taylor & Francis. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Article; Food Biotechnology
Wahab, Roswanira Abdul
Basri, Mahiran
Rahman, Raja Noor Zaliha Raja Abdul
Salleh, Abu Bakar
Rahman, Mohd Basyaruddin Abdul
Chaibakhsh, Naz
Leow, Thean Chor
Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title_full Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title_fullStr Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title_full_unstemmed Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title_short Enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from Geobacillus zalihae
title_sort enzymatic production of a solvent-free menthyl butyrate via response surface methodology catalyzed by a novel thermostable lipase from geobacillus zalihae
topic Article; Food Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686904/
https://www.ncbi.nlm.nih.gov/pubmed/26740782
http://dx.doi.org/10.1080/13102818.2014.978220
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