Characteristics of yeast invertase immobilized on porous cellulose beads.

Abstract:

:Invertase from Candida utilis was immobilized on porous cellulose beads by an ionic-quanidino bond. The immobilized invertase showed optimum activity between pH 4.0 and 5.4, while the free enzyme had a sharp optimum at pH 4.1. Both temperature profiles were fairly similar up to 55 degrees C. However, above this temperature the immobilized enzyme was more stable than the free enzyme. From the temperature data, the activation energies were found to be 7,322 and 4,052 cal/g mol for the free and the immobilized enzyme, respectively. Candida invertase shows characteristics of substrate inhibition. Both the Km and Ki for the free and the immobilized enzymes were determined. The apparent Ki for the immobilized invertase was much higher than the Ki of the free enzyme, suggesting a diffusion effect. Immobilized invertase molecules deep in the pores only see sucrose concentrations much less than the bulk concentrations. Immobilization, thus, offers certain processing advantages in this regard.

journal_name

Biotechnol Bioeng

authors

Dickensheets PA,Chen LF,Tsao GT

doi

10.1002/bit.260190307

subject

Has Abstract

pub_date

1977-03-01 00:00:00

pages

365-75

issue

3

eissn

0006-3592

issn

1097-0290

journal_volume

19

pub_type

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