Alkaline a-L-rhamnosidase from Acrostalagmus luteo-albus: Production, purification and characterization

ROJAS NL; ELGUEA L; FERNANDEZ ME; ORTIZ GE; CONTRERAS ESQUIVEL JC; CAVALITTO SF; VOGET CE; HOURS RA

Congreso; First International Congress on Biotechnology and Bioengineerin; International initiatives for a Sustainable Development; 2008

An enzyme exhibiting α-L-rhamnosidase activity was purifedfrom a culture filtrate of Acrostalagmus luteo-albusgrown on L-rhamnose as the sole carbon source. The α-Lrhamnosidase has a molecular mass of 109 kDa and an isoelectric point of 4.6. The enzyme, was optimally active at pH 8 and 55º C with p-nitrophenyl-α-L-rhamnopyranoside as substrate and showed Km and Vmax values of 3.38 mM and 68.5 U ml-1, respectively. Divalents cations such as Ca+2, Mg+2, Mn+2, and Co+2 showed no effect over enzyme activity, whereas this was completely inhibited by Zn+2 at a concentration of 0.1 mM. Substrate specifity studies showed that α-L-rhamnosidase is active towards hesperidin, naringin and quircitrin.