Next Article in Journal
Pharmacogenetics of OATP Transporters Reveals That SLCO1B1 c.388A>G Variant Is Determinant of Increased Atorvastatin Response
Next Article in Special Issue
Environmental Dependence of Artifact CD Peaks of Chiral Schiff Base 3d-4f Complexes in Soft Mater PMMA Matrix
Previous Article in Journal
A Sweet Killer: Mesoporous Polysaccharide Confined Silver Nanoparticles for Antibacterial Applications
Article Menu

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2011, 12(9), 5797-5814; doi:10.3390/ijms12095797

Role of α-Helical Structure in Organic Solvent-Activated Homodimer of Elastase Strain K

1
Enzyme and Microbial Technology Laboratory, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, UPM Serdang 43400, Selangor, Malaysia
2
Enzyme and Microbial Technology Laboratory, Faculty of Science, Universiti Putra Malaysia, UPM Serdang 43400, Selangor, Malaysia
*
Author to whom correspondence should be addressed.
Received: 18 July 2011 / Revised: 5 August 2011 / Accepted: 11 August 2011 / Published: 9 September 2011
(This article belongs to the Special Issue Applications of Circular Dichroism)
View Full-Text   |   Download PDF [483 KB, 19 June 2014; original version 19 June 2014]   |  

Abstract

Recombinant elastase strain K overexpressed from E. coli KRX/pCon2(3) was purified to homogeneity by a combination of hydrophobic interaction chromatography and ion exchange chromatography, with a final yield of 48% and a 25-fold increase in specific activity. The purified protein had exhibited a first ever reported homodimer size of 65 kDa by SDS-PAGE and MALDI-TOF, a size which is totally distinct from that of typically reported 33 kDa monomer from P. aeruginosa. The organic solvent stability experiment had demonstrated a stability pattern which completely opposed the rules laid out in previous reports in which activity stability and enhancement were observed in hydrophilic organic solvents such as DMSO, methanol, ethanol and 1-propanol. The high stability and enhancement of the enzyme in hydrophilic solvents were explained from the view of alteration in secondary structures. Elastinolytic activation and stability were observed in 25 and 50% of methanol, respectively, despite slight reduction in α-helical structure caused upon the addition of the solvent. Further characterization experiments had postulated great stability and enhancement of elastase strain K in broad range of temperatures, pHs, metal ions, surfactants, denaturing agents and substrate specificity, indicating its potential application in detergent formulation. View Full-Text
Keywords: P. aeruginosa strain K; organic solvent tolerant protease; dimerization; secondary structures P. aeruginosa strain K; organic solvent tolerant protease; dimerization; secondary structures
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Abd. Rahman, R.N.Z.R.; Salleh, A.B.; Basri, M.; Wong, C.F. Role of α-Helical Structure in Organic Solvent-Activated Homodimer of Elastase Strain K. Int. J. Mol. Sci. 2011, 12, 5797-5814.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top