Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis

Hansol Ju; Eunjin Jang; Bum Han Ryu; T Doohun Kim

doi:10.1016/j.biortech.2012.10.016

Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis

Bioresour Technol. 2013 Jan:128:81-6. doi: 10.1016/j.biortech.2012.10.016. Epub 2012 Oct 17.

Authors

Hansol Ju¹, Eunjin Jang, Bum Han Ryu, T Doohun Kim

Affiliation

¹ Department of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749, South Korea.

PMID: 23196225
DOI: 10.1016/j.biortech.2012.10.016

Abstract

A novel type of hydrolase (BL28) from Bacillus licheniformis was identified, expressed in Escherichia coli, characterized, and immobilized for industrial applications. Biochemical characteristics of BL28 were investigated by performing SDS-PAGE, mass spectrometry, enzyme assays, CD spectroscopy, intrinsic fluorescence, and in silico analysis. Furthermore, cross-linked enzyme aggregates (CLEAs) of BL28 were prepared. These CLEA-BL28 aggregates exhibited improved catalytic efficiencies and stabilities compared to free BL28 against harsh conditions of thermal or chemical stress as well as high reusability. The characteristics of the CLEA-BL28 aggregates highlight their great potentials in pharmaceutical and chemical industries.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Bacillus / enzymology*
Enzyme Activation
Enzyme Stability
Hydrolases / chemistry*
Hydrolases / isolation & purification*
Molecular Sequence Data
Substrate Specificity

Substances

Hydrolases