-Glucosidase Activity in Mycoplasma

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Abstract
Strains of three groups of Mycoplasma with different nutritional requirements were analyzed for [beta]-glucosidase activity. The enzyme was found in the cell membrane of Mycoplasma laidlawii strain B and M. gallisepticum strain J, which metabolize carbohydrates; negligible [beta]-glucosidase activity was found in M. hominis strain 07 which does not metabolize carbohydrates. [beta]-Glucosidase in all strains was inactivated by heating at 56[degree] for 30 min. or at 100[degree] for 10 min. With M. laidlawii strain B as the test organism, [beta]-glucosidase was found to possess the following characteristics: pH optimum, 6.8; optimum temperature, 30[degree]; no dialyzable cofactors required; phosphate ions had no effect on activity; enzyme was specific for substrates (glucosides) with [beta] configuration; aglycon of the glucoside must be an aryl group; enzyme exhibited absolute specificity for carbon atoms number 4 and 5 of the glycon. The presence of [beta]-glucosidase in M. laidlawii strain B and M. gallisepticum strain J is assumed to be involved in the synthesis and hydrolysis of carotenyl glycoside and sterol glucoside by these organisms.

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