Optimization and partial characterization of invertase using chitin as solid support

Date

4-2009

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Veronica C. Sabularse

Abstract

TERRENAL, JESSE JOHN L. University of the Philippines Los Banos. 2009 Optimization and Partial Characterization of Immobilized Invertase using Chitin as Solid Support.

Adviser: Dr. Veronica C. Sabularse

Yeast invertase was immobilized using chitin as a solid support. Chitin was isolated from squid pen by immobilization and demineralization. Proximate analysis and scanning electron microscopy (SEM) were conducted to determine the differences in chemical composition and physical attributes of the squid pen and the chitin product. The chitin product appeared as smaller particles than the squid pen particles.

The optimum concentrations of 3,5-aminopropyltriethoxysilane (APTS) and glutaraldehyde to be used in immobilization of invertase on chitin were determined. The optimum amount of APTS was 8% and that of glutaraldehyde was 2.5%. Using these concentrations, the amount of invertase immobilized was 3.74 ing/mL chitin or 93% of the enzyme used. The activity of the immobilized enzyme was compared to that of the free enzyme. Both free and immobilized enzyme exhibited maximal activity at a pH of 4.5, a temperature of 55°C and sucrose concentration of 0.7 M. The activation energy (En) of the free enzyme was 0.0121 KJ/mol while that of the immobilized enzyme was 0.0283 KJ/mol. The kinetic parameters, Michaelis constant, K,,, and maximal velocity, for the free enzyme were 0.050 mM and 222.07 amol/min respectively. The KR, for the immobilized enzyme was 0.084 mM and its Vmax 225.27 ilmol/min. The immobilized invertase was found to be relatively stable towards repeated use arid continuous use.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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