N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase.

Castor oil Esterases Lid domain Lipases TON-LPL Thermococcus onnurineus (strain NA1) Thermomyces lanuginosus (TLIP) rc-TGL

Journal

Biotechnology for biofuels
ISSN: 1754-6834
Titre abrégé: Biotechnol Biofuels
Pays: England
ID NLM: 101316935

Informations de publication

Date de publication:
2019
Historique:
received: 12 10 2018
accepted: 25 04 2019
entrez: 14 5 2019
pubmed: 14 5 2019
medline: 14 5 2019
Statut: epublish

Résumé

Lipolytic enzymes of hyperthermophilic archaea generally prefer small carbon chain fatty acid esters (C TON-LPL and rc-TGL were cloned and overexpressed in Here, we have confirmed the predicted esterase activity of TON-LPL and also performed the lid engineering on TON-LPL which effectively expanded its substrate specificity from monoglycerides to triglycerides. This approach provides a way to engineer other hyperthermophilic esterases into industrially suitable lipases by employing N-terminal domain replacement. The immobilized preparation of rc-TGL has shown significant activity with castor oil and has a potential application in castor oil biorefinery to obtain value-added chemicals.

Sections du résumé

BACKGROUND BACKGROUND
Lipolytic enzymes of hyperthermophilic archaea generally prefer small carbon chain fatty acid esters (C
RESULTS RESULTS
TON-LPL and rc-TGL were cloned and overexpressed in
CONCLUSIONS CONCLUSIONS
Here, we have confirmed the predicted esterase activity of TON-LPL and also performed the lid engineering on TON-LPL which effectively expanded its substrate specificity from monoglycerides to triglycerides. This approach provides a way to engineer other hyperthermophilic esterases into industrially suitable lipases by employing N-terminal domain replacement. The immobilized preparation of rc-TGL has shown significant activity with castor oil and has a potential application in castor oil biorefinery to obtain value-added chemicals.

Identifiants

pubmed: 31080517
doi: 10.1186/s13068-019-1452-5
pii: 1452
pmc: PMC6501381
doi:

Types de publication

Journal Article

Langues

eng

Pagination

110

Déclaration de conflit d'intérêts

The authors declare that they have no competing interests.

Références

Biotechnol Bioeng. 1998 Mar 5;57(5):624-9
pubmed: 10099242
Biochem J. 1999 Oct 1;343 Pt 1:177-83
pubmed: 10493927
Biochemistry. 2000 Jan 18;39(2):413-23
pubmed: 10631003
Biochemistry. 2000 Dec 12;39(49):15071-82
pubmed: 11106485
Microbiol Mol Biol Rev. 2001 Mar;65(1):1-43
pubmed: 11238984
Gene. 2002 Jan 23;283(1-2):107-15
pubmed: 11867217
Appl Environ Microbiol. 2002 Aug;68(8):3925-31
pubmed: 12147492
Biophys J. 2004 May;86(5):2758-64
pubmed: 15111394
J Biol Chem. 2004 Jul 30;279(31):32957-67
pubmed: 15169774
Appl Biochem Biotechnol. 2004 Jul-Sep;118(1-3):155-70
pubmed: 15304746
Biotechnol Lett. 2005 Jun;27(11):743-8
pubmed: 16086253
Science. 2006 Jan 27;311(5760):484-9
pubmed: 16439654
Biochim Biophys Acta. 2006 May;1760(5):820-8
pubmed: 16574328
BMC Bioinformatics. 2008 Jan 23;9:40
pubmed: 18215316
J Microbiol. 2008 Feb;46(1):100-7
pubmed: 18337701
PLoS Comput Biol. 2008 Feb 29;4(2):e1000002
pubmed: 18463696
J Mol Biol. 2009 Jul 24;390(4):672-85
pubmed: 19447113
Methods Enzymol. 2009;463:439-73
pubmed: 19892187
Nat Protoc. 2010 Apr;5(4):725-38
pubmed: 20360767
Chembiochem. 2010 Aug 16;11(12):1635-43
pubmed: 20593436
Enzyme Res. 2011;2011:316939
pubmed: 21760993
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1473-9
pubmed: 22139147
Extremophiles. 2012 Jul;16(4):619-25
pubmed: 22622648
Chem Biol Interact. 2013 Mar 25;203(1):266-8
pubmed: 23010363
Protein Eng Des Sel. 2012 Nov;25(11):689-97
pubmed: 23043134
J Lipid Res. 2014 Jun;55(6):1044-51
pubmed: 24670990
Biomed Res Int. 2014;2014:684506
pubmed: 24783219
Front Microbiol. 2014 Apr 17;5:172
pubmed: 24860555
Appl Environ Microbiol. 2014 Nov;80(22):6870-8
pubmed: 25149523
Int J Mol Sci. 2014 Sep 23;15(9):16885-910
pubmed: 25250909
Biotechnol J. 2015 Sep;10(11):1762-9
pubmed: 26097135
Biol Proced Online. 2016 Jan 13;18:2
pubmed: 26766927
Crit Rev Biotechnol. 2017 May;37(3):309-322
pubmed: 26940154
J Mol Biol. 2016 Jun 5;428(11):2359-2371
pubmed: 27016206
Biochim Biophys Acta Proteins Proteom. 2017 Jan;1865(1):20-27
pubmed: 27693248
Can J Microbiol. 2017 Mar;63(3):179-192
pubmed: 28165765
Front Bioeng Biotechnol. 2017 Mar 09;5:16
pubmed: 28337436
Proteins. 2017 Oct;85(10):1845-1855
pubmed: 28643343
Angew Chem Int Ed Engl. 1998 Jul 3;37(12):1608-1633
pubmed: 29711530

Auteurs

Surabhi Soni (S)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Sneha S Sathe (SS)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Rutuja R Sheth (RR)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Prince Tiwari (P)

3IISER Mohali, Knowledge City, Sector 81, Manauli PO, Sahibzada Ajit Singh Nagar, Punjab 140306 India.

Rajesh-Kumar N Vadgama (RN)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Annamma Anil Odaneth (AA)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Arvind M Lali (AM)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.
2Department of Chemical Engineering, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Sanjeev K Chandrayan (SK)

1DBT Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga East, Mumbai, Maharashtra 400019 India.

Classifications MeSH