Immobilization of isolated and cellular hydrogenase of D. desulfuricans in radiation-polymerized polyacrylamides

Journal Article · Wed Feb 01 04:00:00 EST 1984 · Appl. Biochem. Biotechnol.; (United States)

DOI:https://doi.org/10.1007/BF02798374· OSTI ID:6385960

Ziomek, E; Martin, W G; Williams, R E

Purified hydrogenase from Desulfovibrio desulfuricans was immobilized either by entrapment or absorption onto porous neutral and charged acrylamide beads. Surface absorption and crosslinking on the beads resulted in a high hydrogenase activity and a good immobilization coefficient compared to the enzyme and whole cells entrapped in the same matrix. Maximum enzyme activity (citrate-phosphate buffer) was shifted to pH 6.5 upon immobilization in contrast to 6.0 for the free enzyme and the range of 6-7 for whole cells. Both the purified enzyme and whole cells were most active when held in neutral matrices. Immobilization improved the temperature stability (65 degrees C) and long term storage (4 degrees C) of the hydrogenase activity of both the purified enzyme and whole cells.

• Research Organization: Division of Biological Sciences, National Research Council, Ottawa, Ontario, Canada
• OSTI ID: 6385960
• Journal Information: Appl. Biochem. Biotechnol.; (United States), Journal Name: Appl. Biochem. Biotechnol.; (United States) Vol. 9:1; ISSN ABIBD
• Country of Publication: United States
• Language: English

Related Subjects

38 RADIATION CHEMISTRY, RADIOCHEMISTRY, AND NUCLEAR CHEMISTRY
400600 -- Radiation Chemistry
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ACRYLAMIDE
AMIDES
BACTERIA
CHEMICAL RADIATION EFFECTS
CHEMICAL REACTIONS
CHEMISTRY
DESULFOVIBRIO
ENZYMES
HYDROGENASES
IMMOBILIZED ENZYMES
MICROORGANISMS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC POLYMERS
OXIDOREDUCTASES
POLYAMIDES
POLYMERIZATION
POLYMERS
RADIATION CHEMISTRY
RADIATION EFFECTS
SAMPLE PREPARATION
SULFATE-REDUCING BACTERIA