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Title 

Enzymatic characterization of a soluble aggregate induced by N-terminal extension to a lipolytic enzyme

Authors 

J M ParkMi-Hwa LeeC H KangKi Hoon OhJung-Sook LeeJ H Yoon

Publisher 

Elsevier

Issue Date 

2018

Citation 

Journal of Biotechnology

Keywords 

Active aggregateDissociative activationMetagenomePeptide-Induced aggregationSoluble aggregateThermal dissociation

Abstract 

A self-assembling peptide (27PEP) was isolated from an open reading frame (ORF). The ORF consisted of an unknown functional domain and a catalytic (lipolytic and phospholipolytic) domain (MPlaG) on metagenomic fosmid clone. This extension of 27 amino acids prior to the N-terminus of the catalytic domain (27PEP-MPlaG), starting at Met261, produced an aggregate of high molecular weight (> 700?kDa). Compared with MPlaG, 27PEP-MPlaG showed the same temperature and pH effect for maximum activity but was stable in the presence of inhibitors such as EDTA and PMSF. The 27PEP-MPlaG exhibited lower specific activity than that of MPlaG, but when pre-incubated for 30?min at temperatures between 4 and 100?°C, its activity increased at temperatures greater than 40?°C under alkaline conditions and eventually reached the specific activity level of MPlaG at 60?°C. We experimentally determined that the aggregate caused by 27PEP was dissociated at elevated temperatures resulting in an active catalytic monomer. The 27PEP-indued aggregation may be attractive as application tool for improving or engineering of biocatalysts and biomaterials.

ISSN 

0168-1656

Link 

http://dx.doi.org/10.1016/j.jbiotec.2018.07.008

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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