Study of formaldehyde dehydrogenase from four sources

Date

5-1996

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Myrna S. Rodriguez

Abstract

Formaldehyde dehydrogenase was partially purified from beef and chicken livers, pea seeds ( Pisum sutivum ) and yeast cells (Saccharomyces cerevisiae ). The effect of pH using different buffers, temperature and storage on enzyme stability were determined. Substrate specificity was also determined. The specific activities for the final preparation of beef and chicken liver, pea and yeast enzymes were 5.75, 5.29, 22.83 and 21.44 U/mg protein respectively. Formaldehyde produced higher specific activity than acetaldehyde, ethanol and propanol as substrate in chicken liver enzyme preparation. Highest specific activity in beef liver preparation was observed in formaldehyde followed by acetaldehyde, propanol and ethanol. Specific activity of formaldehyde dehydrogenase from pea seed preparation was highest in formaldehyde then propanol, acetaldehyde and ethanol. Yeast cell preparation has highest specific activity in formaldehyde then ethanol, acetaldehyde and propanol. Chicken and beef liver enzyme preparations exhibited maximum specific activity at 20 °C. Pea and yeast enzyme preparations were most active at 10 °C to 20 °C. The optimum pH for all enzyme preparations was at pH 8.0 All enzyme preparations stored in phosphate buffer have a half life of 10 days. Pea and yeast enzyme preparation stored in distilled water have a half life of 9 days while beef and chicken enzyme preparations have a half life of 7 days.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 1996 C4 H55

Document Type

Thesis

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