Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6490158 | Journal of Biotechnology | 2018 | 26 Pages |
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 (> 700â¯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 30â¯min at temperatures between 4 and 100â¯Â°C, its activity increased at temperatures greater than 40â¯Â°C under alkaline conditions and eventually reached the specific activity level of MPlaG at 60â¯Â°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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Ji-Min Park, Mi-Hwa Lee, Chul-Hyung Kang, Ki-Hoon Oh, Jung-Sook Lee, Jung-Hoon Yoon,