ALKALINE α-L-RHAMNOSIDASE FROM ACROSTALAGMUS LUTEO-ALBUS: PRODUCTION, PURIFICATION AND CHARACTERIZATION.

ROJAS, N.L.; ELGUEA, L; FERNÁNDEZ, M.E.; ORTIZ, G. E; CONTRERAS ESQUIVEL, J.C; CAVALITTO, S.F; VOGET, C.E.; HOURS, R.A

Mexico City, Mexico.

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

Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional

An enzyme exhibiting α-L-rhamnosidase activity was purifed from a culture filtrate of Acrostalagmus luteo-albus grown on L-rhamnose as the sole carbon source. The α-L-rhamnosidase 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.