Mvg. Custodio et al., PRODUCTION AND CHARACTERIZATION OF AN ASPERGILLUS-TERREUS ALPHA-L-RHAMNOSIDASE OF ENOLOGICAL INTEREST, Zeitschrift fur Lebensmittel-Untersuchung und -Forschung, 203(6), 1996, pp. 522-527
Conditions for maximal batch culture production of extracellular alpha
-L-rhamnosidase by Aspergillus terreus have been investigated. Product
ion of the enzyme appeared to be inducible by rhamnose and rutin, reac
hing a maximal level after an incubation period of 162 h when the fung
us was grown at 37 degrees C on either of these compounds as the carbo
n source and on ammonium phosphate as the nitrogen source. Nonionic su
rfactants did not enhance alpha-L-rhamnosidase secretion. Under optima
l conditions, A. terreus produced only one alpha-L-rhamnosidase of app
roximate molecular weight 90 kDa (SDS-PAGE) and isoelectric point of 4
.6. On p-nitrophenyl-alpha-L-rhamnopyranoside as substrate, the enzyme
showed pH and temperature optima of 6-8 and 45-50 degrees C, respecti
vely. Neither divalent cations nor ethylenediaminetetraacetate (EDTA)
inhibited or stimulated enzyme activity. The enzyme was active at the
concentrations of glucose found in must or of ethanol in wine.