Expression and Partial Purification of an Alkalophilic a-L-rhamnosidase from Acremonium murorum in Submerged Cultures

ROJAS, N.L; FERNANDEZ, M.E.; ELGEA, L; CONTRERAS ESQUIVEL, J.C; CAVALITTO, S.F.; HOURS, R.A

Querétaro, México

Congreso; Food Science and Food Biotechnology in Developing Countries; 2008

Sociedad Mexicana de Biotecnología y Bioingeniería

<!-- /* Style Definitions */ p.MsoNormal, li.MsoNormal, div.MsoNormal {mso-style-parent:""; margin:0cm; margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman"; mso-ansi-language:EN-US;} @page Section1 {size:612.0pt 792.0pt; margin:70.85pt 3.0cm 70.85pt 3.0cm; mso-header-margin:36.0pt; mso-footer-margin:36.0pt; mso-paper-source:0;} div.Section1 {page:Section1;} --> __________________________________________________________________ Rhamnosidase (EC 3.2.1.40) catalyzes the hydrolysis of glycosidic bonds in rhamnosides which results in free rhamnose. Acremomium murorum produces an a-L- rhamnosidase and a b-D-glucosidase active in alkaline conditions. A. murorum was grown in media with different carbon and energy sources. Rhase was partially purified from a culture supernatant. Among studied CES, rhamnose is the most convenient for the production of Rhase with the lowest Gluse content.