Partial purification and characterization of pectinases of Aspergillus ficuum isolated from pomelo

Date

4-1993

Degree

Bachelor of Science in Agricultural Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Teresita M. Espino

Abstract

Crude pectic enzyme extract obtained by solid substrate fermentation in enamelled trays were isolated from the culture medium of Aspergillus ficuum from pomelo.. The purification of the crude enzyme extract included 70% ammonium sulfate precipitation, calcium phosphate gel adsorption and gel chromatography on Sephadex 8-75. Two major PG peaks and two PTE peaks were obtained after gel chromatography on Sephadem 8-75. For PTE fractions I and II, the yields were 17.3% and 20.4% respectively while the purification folds were 182.70 m in the former and 485.60 x in the latter. However, the total yields and purification folds were very be for PG fractions I and II.

The optimum temperatures for polygalacturonase activities of peaks I and II were 60oC and 50oC respectively. Polygalacturonase peaks I and II were most stable at 30oC and 40oC respectively. In the case of pectin transeliminase peaks I and II, their optimum temperatures for enzyme activities were 40oC and 50oC respectively. PTE I was most stable at :10-400 while PTE II was most stable at 50oC.

The optimum pH for both PG I and PS II were 2.5. Polygalacturonase peaks and II were most stable at pH 2.5 and 3.0 respectively. For pectin transeliminase peaks, optimum activities were pH 3.0 for PTE I and pH 3.5 for PTE If. PTE I and PTE II were most stable at pH 2.0 and pH 2.5 respectively.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 1993 A13 P47

Document Type

Thesis

This document is currently not available here.

Share

COinS