Electronic Journal of Polish Agricultural Universities (EJPAU) founded by all Polish Agriculture Universities presents original papers and review articles relevant to all aspects of agricultural sciences. It is target for persons working both in science and industry,regulatory agencies or teaching in agricultural sector. Covered by IFIS Publishing (Food Science and Technology Abstracts), ELSEVIER Science - Food Science and Technology Program, CAS USA (Chemical Abstracts), CABI Publishing UK and ALPSP (Association of Learned and Professional Society Publisher - full membership). Presented in the Master List of Thomson ISI.
2012
Volume 15
Issue 4
Topic:
Biotechnology
ELECTRONIC
JOURNAL OF
POLISH
AGRICULTURAL
UNIVERSITIES
Jankiewicz U. , Frk M. 2012. PROTEOLYTIC ACTIVITY OF PSEUDOMONAS CHLORORAPHIS 5N ISOLATED FROM RHIZOSPHERE SOIL, EJPAU 15(4), #03.
Available Online: http://www.ejpau.media.pl/volume15/issue4/abs-03.html

PROTEOLYTIC ACTIVITY OF PSEUDOMONAS CHLORORAPHIS 5N ISOLATED FROM RHIZOSPHERE SOIL

Urszula Jankiewicz1, Magdalena Frk2
1 Department of Biochemistry, Warsaw University of Life Sciences – SGGW, Poland
2 Department of Biochemistry, Department of Enviromental Improvement Warsaw University of Life Sciences, Poland

 

ABSTRACT

A Gram-negative bacterial strain characterized by high proteolytic activity was isolated from rhizosphere soil under winter wheat. Morphological and biochemical testing as well as analysis of 16S rRNA gene sequence identified the strain as Pseudomonas chlororaphis. In this study an extracellular endopeptidase synthesized by the strain was purified and characterized. The enzyme showed highest activity at pH 11 and at temperature 42C. The molecular weight determined by SDS-PAGE was approx. 51 kDa. The studied endopeptidase was characterized by low thermal stability in the 37-45C range. The activity of the enzyme was strongly inhibited by specific metallopeptidase inhibitors, which allowed classifying the studied protein as a metalloendopeptidase. Ca2+ and Mg2+ ions stimulated the activity of the enzyme, whereas Mn2+, Co2+ and Cu2+ ions inhibited it.

Key words: endopeptidase, metallopeptidase, purification.


Urszula Jankiewicz
Department of Biochemistry, Warsaw University of Life Sciences – SGGW, Poland
Nowoursynowska 159
02-776 Warsaw
Poland
email: urszula_jankiewicz@sggw.pl

Magdalena Frk
Department of Biochemistry, Department of Enviromental Improvement
Warsaw University of Life Sciences, Poland

email: magdalena_frak@sggw.pl

Responses to this article, comments are invited and should be submitted within three months of the publication of the article. If accepted for publication, they will be published in the chapter headed 'Discussions' and hyperlinked to the article.