Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532015000200247 |
Resumo: | 1,3-Diglyceride (1,3-DG) has attracted considerable attention as a healthful food oil component. In this study, we reported a novel method to synthesis of 1,3-DG via glycerolysis of triglyceride (TG) catalyzed by whole-cell lipase from a new isolated strain, Aspergillus niger GZUF36. The glycerolysis products include major diglyceride and minor monoglyceride. To improve yield of 1,3-DG, the optimized medium for the strain was obtained by combination of single-factor experiments, Plackett-Burman (PB), the steepest ascent and Box-Behnken design (BBD). Using the optimized medium, yield of 1,3-DG synthesized by the whole-cell lipase was 26.90 mol% and 1.42-fold yield was improved. The optimized medium lays the foundation for further studies of the reaction system for synthesis of 1,3-DG. The whole-cell catalyzed-glycerolysis process represents a significant advance toward achieving economical production of 1,3-DG at industrial scale. |
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Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization1,3-diglyceridescreeningAspergillus niger GZUF36medium optimizationwhole-cell lipase1,3-Diglyceride (1,3-DG) has attracted considerable attention as a healthful food oil component. In this study, we reported a novel method to synthesis of 1,3-DG via glycerolysis of triglyceride (TG) catalyzed by whole-cell lipase from a new isolated strain, Aspergillus niger GZUF36. The glycerolysis products include major diglyceride and minor monoglyceride. To improve yield of 1,3-DG, the optimized medium for the strain was obtained by combination of single-factor experiments, Plackett-Burman (PB), the steepest ascent and Box-Behnken design (BBD). Using the optimized medium, yield of 1,3-DG synthesized by the whole-cell lipase was 26.90 mol% and 1.42-fold yield was improved. The optimized medium lays the foundation for further studies of the reaction system for synthesis of 1,3-DG. The whole-cell catalyzed-glycerolysis process represents a significant advance toward achieving economical production of 1,3-DG at industrial scale.Sociedade Brasileira de Química2015-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532015000200247Journal of the Brazilian Chemical Society v.26 n.2 2015reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0103-5053.20140261info:eu-repo/semantics/openAccessLi,CuiqinLi,LanxiangZhou,HuanjingXia,ChaoshuangHe,Lapingeng2015-10-26T00:00:00Zoai:scielo:S0103-50532015000200247Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2015-10-26T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
title |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
spellingShingle |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization Li,Cuiqin 1,3-diglyceride screening Aspergillus niger GZUF36 medium optimization whole-cell lipase |
title_short |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
title_full |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
title_fullStr |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
title_full_unstemmed |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
title_sort |
Improving Yield of 1,3-Diglyceride by Whole-Cell Lipase from A. Niger GZUF36 Catalyzed Glycerolysis via Medium Optimization |
author |
Li,Cuiqin |
author_facet |
Li,Cuiqin Li,Lanxiang Zhou,Huanjing Xia,Chaoshuang He,Laping |
author_role |
author |
author2 |
Li,Lanxiang Zhou,Huanjing Xia,Chaoshuang He,Laping |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Li,Cuiqin Li,Lanxiang Zhou,Huanjing Xia,Chaoshuang He,Laping |
dc.subject.por.fl_str_mv |
1,3-diglyceride screening Aspergillus niger GZUF36 medium optimization whole-cell lipase |
topic |
1,3-diglyceride screening Aspergillus niger GZUF36 medium optimization whole-cell lipase |
description |
1,3-Diglyceride (1,3-DG) has attracted considerable attention as a healthful food oil component. In this study, we reported a novel method to synthesis of 1,3-DG via glycerolysis of triglyceride (TG) catalyzed by whole-cell lipase from a new isolated strain, Aspergillus niger GZUF36. The glycerolysis products include major diglyceride and minor monoglyceride. To improve yield of 1,3-DG, the optimized medium for the strain was obtained by combination of single-factor experiments, Plackett-Burman (PB), the steepest ascent and Box-Behnken design (BBD). Using the optimized medium, yield of 1,3-DG synthesized by the whole-cell lipase was 26.90 mol% and 1.42-fold yield was improved. The optimized medium lays the foundation for further studies of the reaction system for synthesis of 1,3-DG. The whole-cell catalyzed-glycerolysis process represents a significant advance toward achieving economical production of 1,3-DG at industrial scale. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-02-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532015000200247 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532015000200247 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.5935/0103-5053.20140261 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.26 n.2 2015 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318176946618368 |