Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Lipases for use in industrial biocatalysis: Specificity of selected structural groups of lipases
Show others and affiliations
2010 (English)In: Journal of Molecular Catalysis B: Enzymatic, ISSN 1381-1177, E-ISSN 1873-3158, Vol. 65, no 1-4, 18-23 p.Article in journal (Refereed) Published
Abstract [en]

Lipases for biocatalysis The substrate specificity of a selected group of lipases was investigated. The enzymes selected were from four structural groups. Group 1: lipases having wide alcohol binding cleft but a narrow acyl binding cleft (Rhizomucor miehei lipase. Thermomyces lanuginosus lipase. Fusarium oxysporum lipase); Group 2: lipases which exhibit strong restriction on the acid part having a narrow tunnel to accommodate the acyl group but wider alcohol binding site (Candida antarctica A, Candida rugosa lipase); Group 3: lipases having wide acyl binding cleft but narrow alcohol binding cleft (C. antarctica lipase B, Ustilago maydis lipase), and Group 4: having wider alcohol and wider acyl binding clefts (Fusarium solani pisi cutinase, Humicola insolens cutinase). Owing to the wide substrate specificity and higher expression levels in recombinant host, these lipases have tremendous importance for hydrolysis and synthesis reactions. Various substrates with substitutions on the alcohol and/or the acid part of the ester molecule were selected. The experimental results support the classification of lipases on the basis of their binding sites. For substrates with heavy alcohol side, C. Antarctica lipase A and R. miehei lipase type enzymes gave the highest extent of hydrolysis, while for acid heavy substrates the highest conversions were shown by C. antarctica lipase B. It is noteworthy that the acid heavy substrates which had aromatic side chains were hydrolyzed only by C. antarctica lipase B type of enzymes. Lipases were found to be more active on the alcohol-substituted substrates than acid-substituted substrates. (C) 2010 Elsevier B.V. All rights reserved.

Place, publisher, year, edition, pages
2010. Vol. 65, no 1-4, 18-23 p.
Keyword [en]
Lipase, Biocatalysis, Substrate specificity, Enantio selectivity
National Category
Biochemistry and Molecular Biology Biochemistry and Molecular Biology Physical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-29690DOI: 10.1016/j.molcatb.2010.01.002ISI: 000278926300004Scopus ID: 2-s2.0-77952583396OAI: oai:DiVA.org:kth-29690DiVA: diva2:401831
Note
QC 20110304Available from: 2011-03-04 Created: 2011-02-11 Last updated: 2017-12-11Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus

Search in DiVA

By author/editor
Chaterjee, Robin
By organisation
Biochemistry
In the same journal
Journal of Molecular Catalysis B: Enzymatic
Biochemistry and Molecular BiologyBiochemistry and Molecular BiologyPhysical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 88 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf