Isolation and purification of neutral protease from Bacillus subtilis (Ehrenberg) cohn (BOITECH 1333)

Date

3-1992

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Teresita M. Espino

Abstract

ABSTRACT

OBERES, ALMA P. University of the Philippines Los Banos larch, 1992. Isolation and Purification of Neutral Protease for Bacillus subtilis (Ehrenberg) Cohn (Biotech 1333).

Adviser: Dr. Teresita M. Espino

A neutral protease was isolated from the culture supernatant of Bacillus subtilis (Ehrenberg) Cohn (Biotech 1333). The neutral protease was purified through ammonium sulfate precipitation, acetone fractionation, CM-cellulose column chromatography and DEAE-Toyopearl column chromatography. The neutral protease fraction showed a single protein band after polyacrylamide disc gel electrophoresis. Enzyme assay of the single protein band showed neutral protease activity. The molecular weights of the neutral protease subunits were 39000 and 32000 daltons as obtained from SDS-polyacrylamide gel electrophoresis. The neutral protease activity was optimum at pH 7.5 and at 40 'C. It was stable at pH 4.5 to 9.2 and at temperature range of 30 to 60 'C.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 1992 C4 O24

Document Type

Thesis

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