Production and Properties of Bacterial &glucuronidase

Hydrolysis of glucuronides is a prerequisite for the quantitative determination or the isolation of a number of physiologically important compounds which are conjugated with glucuronic acid in the animal body. The use of acid for this hydrolysis has frequently brought about chemical alteration of the product under study (14). The need for a hydrolytic agent which is specific and sufficiently mild to preclude the possibility of chemical alteration has led to the investigation of biological catalysts (enzymes). Obviously, an enzyme possessing the capacity to hydrolyze glucuronides at a low temperature and approximate neutrality should fulfil these requirements. Preparations containing such activity have been obtained from both mammalian and bacterial sources. Fishman et al. (5-7) and others (8, 9) have published reports on the preparation and purification of the enzyme from animal sources, and Buehler et al. (10) have presented details of the preparation and use of p-glucuronidase from Escherichia coli. The experimental work which is reported in this paper defines more clearly the conditions for the production of the latter and describes some of the characteristics of the partially purified product.