Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input
Enzymatic synthesis of 6-O-D-glucosyldecanoate in tert-butanol was performed using substrates D-glucose as acyl acceptor and decanoic acid as acyl donor. Candida antarctica lipase B (Novozyme 435) was used as the catalyst in the esterification process. Box Behnken of response surface methodology (RS...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Published: |
2011
|
| Subjects: |
| _version_ | 1796945920917504000 |
|---|---|
| author | Han, J. Annuar, M.S.M. Ariffin, M.F.K. Gumel, A.M. Ibrahim, S. Heidelberg, T. Bakar, B. Hossain, A.B.M.S. Sharifuddin, Y. |
| author_facet | Han, J. Annuar, M.S.M. Ariffin, M.F.K. Gumel, A.M. Ibrahim, S. Heidelberg, T. Bakar, B. Hossain, A.B.M.S. Sharifuddin, Y. |
| author_sort | Han, J. |
| collection | UM |
| description | Enzymatic synthesis of 6-O-D-glucosyldecanoate in tert-butanol was performed using substrates D-glucose as acyl acceptor and decanoic acid as acyl donor. Candida antarctica lipase B (Novozyme 435) was used as the catalyst in the esterification process. Box Behnken of response surface methodology (RSM) was used in the optimization of selected parameters viz. reaction temperature, reaction time, substrate ratio and amount of enzyme loading. Substrate ratio was found to be the sole significant main effect while the second-order interaction between reaction time and immobilized enzyme loading was found to be a significant interaction factor. Optimized conditions for the process were: substrate molar ratio 1 (mole acyl donor-to-mole acyl acceptor), 7.5 g·L-1 immobilized enzyme loading, reaction temperature 55°C and time of 14.2 hours. When a mixed-flow impeller with downward pumping mode was used in a stirred tank reactor, minimum power input at 6.8 kW·kg-1 solvent was sufficient for an improved yield of 0.77 g glucosyl decanoate per g glucose. The reaction product composed solely of monoester with sugar acylation occurring at 6-OH primary group of D-glucose where 60 (mole) of the product was 6-O-β-D-glucosyldecanoate and 40 (mole) 6-O-α-D-glucosyldecanoate. |
| first_indexed | 2024-03-06T05:23:50Z |
| format | Article |
| id | um.eprints-9431 |
| institution | Universiti Malaya |
| last_indexed | 2024-03-06T05:23:50Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | um.eprints-94312017-07-03T08:50:14Z http://eprints.um.edu.my/9431/ Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input Han, J. Annuar, M.S.M. Ariffin, M.F.K. Gumel, A.M. Ibrahim, S. Heidelberg, T. Bakar, B. Hossain, A.B.M.S. Sharifuddin, Y. T Technology (General) TA Engineering (General). Civil engineering (General) Enzymatic synthesis of 6-O-D-glucosyldecanoate in tert-butanol was performed using substrates D-glucose as acyl acceptor and decanoic acid as acyl donor. Candida antarctica lipase B (Novozyme 435) was used as the catalyst in the esterification process. Box Behnken of response surface methodology (RSM) was used in the optimization of selected parameters viz. reaction temperature, reaction time, substrate ratio and amount of enzyme loading. Substrate ratio was found to be the sole significant main effect while the second-order interaction between reaction time and immobilized enzyme loading was found to be a significant interaction factor. Optimized conditions for the process were: substrate molar ratio 1 (mole acyl donor-to-mole acyl acceptor), 7.5 g·L-1 immobilized enzyme loading, reaction temperature 55°C and time of 14.2 hours. When a mixed-flow impeller with downward pumping mode was used in a stirred tank reactor, minimum power input at 6.8 kW·kg-1 solvent was sufficient for an improved yield of 0.77 g glucosyl decanoate per g glucose. The reaction product composed solely of monoester with sugar acylation occurring at 6-OH primary group of D-glucose where 60 (mole) of the product was 6-O-β-D-glucosyldecanoate and 40 (mole) 6-O-α-D-glucosyldecanoate. 2011 Article PeerReviewed Han, J. and Annuar, M.S.M. and Ariffin, M.F.K. and Gumel, A.M. and Ibrahim, S. and Heidelberg, T. and Bakar, B. and Hossain, A.B.M.S. and Sharifuddin, Y. (2011) Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input. Biotechnology & Biotechnological Equipment, 25 (4). pp. 2642-2651. ISSN 1310-2818, DOI https://doi.org/10.5504/Bbeq.2011.0092 <https://doi.org/10.5504/Bbeq.2011.0092>. http://www.scopus.com/inward/record.url?eid=2-s2.0-84856428688&partnerID=40&md5=3c4c1e23ab684dc9e56b22ba3999d75f http://www.diagnosisp.com/dp/journals/viewarticle.php?journalid=1&archive=0&issueid=34&articleid=1202 Doi 10.5504/Bbeq.2011.0092 |
| spellingShingle | T Technology (General) TA Engineering (General). Civil engineering (General) Han, J. Annuar, M.S.M. Ariffin, M.F.K. Gumel, A.M. Ibrahim, S. Heidelberg, T. Bakar, B. Hossain, A.B.M.S. Sharifuddin, Y. Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title | Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title_full | Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title_fullStr | Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title_full_unstemmed | Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title_short | Lipase-catalyzed synthesis of 6-o-d-glucosyldecanoate in tert-butanol: reaction optimization and effect of mixing power input |
| title_sort | lipase catalyzed synthesis of 6 o d glucosyldecanoate in tert butanol reaction optimization and effect of mixing power input |
| topic | T Technology (General) TA Engineering (General). Civil engineering (General) |
| work_keys_str_mv | AT hanj lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT annuarmsm lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT ariffinmfk lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT gumelam lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT ibrahims lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT heidelbergt lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT bakarb lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT hossainabms lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput AT sharifuddiny lipasecatalyzedsynthesisof6odglucosyldecanoateintertbutanolreactionoptimizationandeffectofmixingpowerinput |