Resumen

SOLIS-BADILLO, E.; MAYORGA-REYES, L.; AZAOLA-ESPINOSA, A.  y  GUTIERREZ-NAVA, A.. Identification of β-galactosidase, β-fructofuranosidase and glycosiltransferase enzymes from Cellulomonas flavigena when grown in several carbon sources. Rev. Mex. Ing. Quím [online]. 2014, vol.13, n.2, pp.583-593. ISSN 1665-2738.

The genus Cellulomonas is a cellulose degrading bacteria which produce a wide variety of glucanases, mainly cellulases and hemicellulases with industrial applications. C. flavigena has the ability to grow on carbon sources that are not derived from lignocellulosic wastes such as lactose, sucrose and raftilose. In this study, when C. flavigena was cultured on lactose and sucrose, the cell production was approximately 2 mg/mL, and when was cultured on raftilose, it reached 1 mg/mL. The hydrolytic activity of β-galactosidase and β-fructofuranosidase enzymes were tested in the intra and extra cellular fractions where the highest activity was found in the intracellular fraction using raftilose as substrate, nevertheless using lactose as substrate the activity was significantly low. The protein profiles of the intracellular extracts presented great quantity of bands in the different substrates used as carbon sources of carbon. Probably the synthesis of intracellular enzymes is not regulated and the cell expresses its whole potential. In addition the presence of the gene β-galactosidase was identified.

Palabras llave : Cellulomonas flavigena; β-galactosidase; β-fructofuranosidase; bifunctionality.

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