Partial characterization of peroxidase in sorghum [Sorghum bicolor L.) moench]

Date

10-1990

Degree

Bachelor of Science in Biology

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Evelyn Mae Tecson-Mendoza

Abstract

Partial characterization of the enzyme of the peroxidase (donor H2O2 oxidoreductase; E. C. 1.11.1.7) from sorghum [Sorghum bicolor (L.) Moench] was conducted. Optimum activity was attained at pH 7.0 and from 25 to 30°C. In substrate kinetics a Km value of 0.54% H.O. was obtained from Lineweaver-Burk graph and a Vmax value of 1.95 abs/min. On the other hand. a Km value of 0.28% H.O. was obtained from Michaelis Menten graph and a Vmax value of 1.13 abs/min. Michaelis Menton graph lad A regular hyperbolic shape. The enzyme when incubated at 0 to 40°C for 30 min retained its full activity. the enzyme retained its optimum catalytic ability during five days of storage at 5 9°C and drastically decreased afterwards.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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