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Title 

Recombinant lipase engineered with amphipathic and coiled-coil peptides

 

양친매성 펩타이드와 중합 펩타이드를 이용한 기능이 개선된 리파아제

Authors 

K S YangBong Hyun SungM K ParkJ H LeeK J LimS C ParkS J KimH K KimJung Hoon SohnH M KimS C Kim

Publisher 

American Chemical Society

Issue Date 

2015

Citation 

ACS Catalysis, vol. 5, no. 8, pp. 5016-5025

Keywords 

accessibilityamphipathic peptidebiocatalysisbiodieselcatalytic activitycoiled-coil peptideenzyme engineeringlipase

Abstract 

Lipases have been utilized industrially to produce biodiesel, oleochemicals, and pharmaceuticals. Many efforts such as metagenomics, directed evolution, and enzyme immobilization have been devoted to enhance the lipase activity. Here, we designed a recombinant lipase, NKC-M37-MAT, that was generated by incorporating an N-terminal amphipathic peptide (NKC) and a C-terminal coiled-coil peptide (MAT) into Photobacterium lipolyticum M37 lipase. The hydrophobic face of NKC improve the accessibility (Km), and catalytic efficiency (Kcat/Km) of the soluble lipase toward the hydrophobic substrate and tetrameric MAT further enhanced lipase catalytic activity (U/mg) through cooperative binding to its substrate such that the catalytic activity (U/mg) of NKC-M37-MAT was increased by a maximum of 54-fold compared with the wild-type, which decreased the biodiesel production time 5-fold from 30 to 6 h. This novel approach shows promise as a platform technology to increase lipase catalytic efficiency for industrial-scale production of biodiesel and biochemicals synthesized from hydrophobic substrates.

ISSN 

2155-5435

Link 

http://dx.doi.org/10.1021/cs502079g

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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