Partial Purification and Characterization of an Alkalophilic a -L-Rhamnosidase from Verticillium tenerum

ROJAS, N. L.; BLANCO FERNANDEZ, M.D; CAVALITTO, S. F.; VOGET, C. E; HOURS, R. A

Saltillo, Mexico

Congreso; Segundo Congreso Internacional Food Science and Food Biotechnology in Developing Countries; 2006

Sociedad Mexicana de Biotecnología y Bioingeniería.

A crude extract of V. tenerum was purified through chromatographic techniques and, as result, a-Rha was partially purified, but no satisfactory separation of a-Rha from b-Glu could be obtained. In order to determine the enzyme pH and temperature stability, a Doehlert design was used to represent the combined effects by means of a polynomial model. In this assay, we noticed that b-Glu was inactivated after incubating the final extract (3 h, at 48°C), while a-Rha remained intact. Heat inactivation allows to obtain active a-rha without b-Glu interferences. (Key words: a-rhamnosidase, b-glucosidase, enzyme stability, Verticillum tenerum)