Recombinant lipase engineered with amphipathic and coiled-coil peptides = 양친매성 펩타이드와 중합 펩타이드를 이용한 기능이 개선된 리파아제

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Title
Recombinant lipase engineered with amphipathic and coiled-coil peptides = 양친매성 펩타이드와 중합 펩타이드를 이용한 기능이 개선된 리파아제
Author(s)
K S Yang; Bong Hyun Sung; M K Park; J H Lee; K J Lim; S C Park; S J Kim; H K Kim; Jung Hoon Sohn; H M Kim; S C Kim
Bibliographic Citation
ACS Catalysis, vol. 5, no. 8, pp. 5016-5025
Publication Year
2015
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.
Keyword
accessibilityamphipathic peptidebiocatalysisbiodieselcatalytic activitycoiled-coil peptideenzyme engineeringlipase
ISSN
2155-5435
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/cs502079g
Type
Article
Appears in Collections:
Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
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