Purification and partial characterization of chitin deacetylase from Planococcus sp.

Date

10-1997

Degree

Bachelor of Science in Agricultural Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Ernesto J Del Rosario

Co-adviser

Ma. Jamela Revilleza

Committee Member

Evamarie Capareda

Abstract

Chitin deacetylase (EC.3.1.1.41) is an enzyme that catalyzes the hydrolysis of the N-acetamido groups of chitin forming chitosan. The enzyme was isolated from the liquid culture of Planococcus sp. Optimum production of enzyme was at pH 7.0 after 28 hours of fermentation. A 46.9 purification fold was obtained when the enzyme was purified by sequential ammonium sulfate fractionation and Sephadex G-100 gel chromatography. The enzyme has a molecular weight of 70 kD after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). With colloidal chitin as substrate, optimum activity and temperature were obtained at pH 6.0 and 50°C respectively.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 1997 A13 M38

Document Type

Thesis

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