Hydrolysis of cellobiose by immobilized {beta}-glucosidase entrapped in maintenance-free gel spheres

Conference · Tue Dec 31 04:00:00 EST 1991

OSTI ID:431586

Woodward, J ^[1]; Clarke, K M ^[2]

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1. Oak Ridge National Lab., TN (United States)
2. Marquette Univ. High School, Milwaukee, WI (United States)

A crude preparation of Aspergillus niger {beta}-glucosidase (27.5 cellobiase U/mg protein at 40{degrees}C, pH 5.0) was immobilized on concanavalin A-Sepharose (CAS). The cellobiase activity of the immobilized enzyme was 1334 U/mg dried CAS or 108 U/mL CAS gel. The {beta}-glucosidase-CAS complex was entrapped within crosslinked propylene glycol alginate/bone-geletin gel spheres that possessed between 0.67 and 2.35 cellobiase U/mL spheres, depending on their size. The effect of cellobiose concentration (10-300 mM) on the activity of native, immobilized, and gel-entrapped enzyme was determined. It was shown that concentrations of cellobiose between 10 and 180 mM were not inhibitory to the entrapped enzyme, although inhibition was found to occur with the native and immobilized enzyme. Exogenous ion addition was not necessary to maintain the structural integrity of the spheres, which were stable for 4 d at 40{degrees}C.

• Research Organization: Oak Ridge National Lab., TN (United States); Badger Engineers, Inc., Tampa, FL (United States); Solar Energy Research Inst., Golden, CO (United States)
• OSTI ID: 431586
• Report Number(s): CONF-900512--
• Country of Publication: United States
• Language: English

Related Subjects

09 BIOMASS FUELS
55 BIOLOGY AND MEDICINE
BASIC STUDIES
ASPERGILLUS
BIOMASS
BIOTECHNOLOGY
CELLOBIOSE
ENZYME ACTIVITY
GLUCOSIDASE
HYDROLYSIS
INHIBITION
SPHERES