Saccharification and Isomerization by GA and GI 193
Applied Biochemistry and Biotechnology Vol. 102–103, 2002 193
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Effect of pH on Simultaneous Saccharification
and Isomerization by Glucoamylase
and Glucose Isomerase
ABHA MISHRA* AND MEERA DEBNATH (DAS)
School of Biochemical Engineering, Institute of Technology,
Banaras Hindu University, Varanasi 221005, India,
E-mail: misrabha91@rediffmail.com
Abstract
pH and temperature play critical roles in multistep enzymatic conver-
sions. In such conversions, the optimal pH for individual steps differs greatly.
In this article, we describe the production of glucoamylase (from Aspergillus
oryzae MTCC152 in solid-state fermentation) and glucose isomerase (from
Streptomyces griseus NCIM2020 in submerged fermentation), used in indus-
tries for producing high-fructose syrup. Optimum pH for glucoamylase was
found to be 5.0. For glucose isomerase, the optimum pH ranged between 7.0
and 8.5, depending on the type of buffer used. Optimum temperature for
glucoamylase and glucose isomerase was 50 and 60°C, respectively. When
both the enzymatic conversions were performed simultaneously at a com-
promised pH of 6.5, both the enzymes showed lowered activity. We also
studied the kinetics at different pHs, which allows the two-step reaction to
take place simultaneously. This was done by separating two steps by a thin
layer of urease. Ammonia generated by the hydrolysis of urea consumed the
hydrogen ions, thereby allowing optimal activity of glucose isomerase at an
acidic pH of 5.0.
Index Entries: Glucoamylase; glucose isomerase; Aspergillus oryzae; Strep-
tomyces griseus.
Introduction
In multienzyme systems, the product of one enzymatic reaction
becomes the substrate for the other. One such example is the production of
high-fructose syrup from low-cost starchy materials. High-fructose syrup,
an equilibrium mixture of glucose and fructose, is approximately one to
three times sweeter than sucrose. It is preferred in the food industry because
it does not pose a problem of crystallization, as happens with sucrose.