CHARACTERIZATION OF AN INTRACELLULAR BETA-GLUCOSIDASE FROM STREPTOMYCES-RETICULI

Autor(en): HEUPEL, C
SCHLOCHTERMEIER, A
SCHREMPF, H 
Stichwörter: BETA-GLUCOSIDASES; Biotechnology & Applied Microbiology; CELLOBIOSE; CELLULASE; CLOSTRIDIUM-THERMOCELLUM; ENZYMES; METABOLISM; PROTEINS; PURIFICATION; SPOROTRICHUM-PULVERULENTUM; STREPTOMYCES-RETICULI
Erscheinungsdatum: 1993
Herausgeber: BUTTERWORTH-HEINEMANN
Journal: ENZYME AND MICROBIAL TECHNOLOGY
Volumen: 15
Ausgabe: 2
Startseite: 127
Seitenende: 132
Zusammenfassung: 
Streptomyces reticuli hydrolyzes cellobiose to glucose by mycelia-associated, extra- and intracellular beta-glucosidase activities during cultivation with crystalline cellulose (Avicel) or cellobiose as carbon source. One intracellular beta-glucosidase was purified to near homogeneity by the use of a fast protein liquid chromatography system combined with several ion-exchange and hydrophobic-interaction columns. The unglycosylated enzyme has an apparent molecular weight of 50 kDa and an isoelectric point of 4.5, and shows optimal activity at pH 7 and 40-degrees-C. It can be stimulated by CaCl2, MgSO4, or cellobiose, and is inhibited by glucose, glucono-lactone, or histidine, but not by imidazole. The beta-glucosidase hydrolyzes p-nitrophenyl-beta-D-gluco-pyranoside, cellobiose, and cellodextrins. The release of glucose from cellooligomers decreases in proportion to their lengths.
ISSN: 01410229
DOI: 10.1016/0141-0229(93)90036-2

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