Factors influencing β‐galactosidase activity ofAeromonas caviae

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Abstract
Aeromonas caviae, often reported to be associated with diarrhoeal patients, elaborates several virulence factors as well as catabolic enzymes such as xylanase and β‐galactosidase. Studies on the kinetics of growth of A. caviae and synthesis of β‐galactosidase suggested that the activity was cell associated and reached a peak during the late logarithmic phase of growth. The optimum pH for β‐galactosidase activity was 7.0 and required Ca2+ and glutathione for enhancement of its activity; IPTG also slightly improved the activity. Aerobic cultivation of A. caviae in LB containing glucose, fructose, maltose and sucrose completely inhibited the activity possibly due to acetic acid production. Addition of 100 mM cAMP to the media containing glucose (0.25%, w/v) restored the relative activity by 8.8%; however, the final pH of the media remained acidic. Aerobic growth of A. caviae with other carbon sources did not affect β‐galactosidase activity, probably as there was no acid production and thereby the final pH of the media unaltered. Arabinose, xylose and galactose induced the A. caviae β‐galactosidase activity by several folds and lactose moderately enhanced its activity.

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