Immobilization of active hydrogenases by encapsulation in polymeric porous gels

Nano Letters

Volumn 5, Issue 10, 2005, Pages 2085-2087

  Elgren, Timothy E ^b   Zadvorny, Oleg A ^a   Brecht, Eric ^a   Douglas, Trevor ^a   Zorin, Nikolay A ^c   Maroney, Michael J ^d   Peters, John W ^a  

^a MONTANA STATE UNIVERSITY   (United States)

^b HAMILTON COLLEGE   (United States)

^c INSTITUTE OF BASIC BIOLOGICAL PROBLEMS   (Russian Federation)

^d UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC MATERIALS; NANOSCOPIC CONFINEMENT; PROTEOLYTIC DIGESTION;

CATALYSIS; ENCAPSULATION; POLYMERS; POROUS MATERIALS;

SILICA GEL;

HYDROGENASE; IMMOBILIZED ENZYME; NANOMATERIAL; POLYMER;

ARTICLE; CHEMISTRY; CLOSTRIDIUM; ENZYME STABILITY; ENZYMOLOGY; GEL; MICROCAPSULE; TEMPERATURE; THIOCAPSA ROSEOPERSICINA;

CAPSULES; CLOSTRIDIUM; ENZYME STABILITY; ENZYMES, IMMOBILIZED; GELS; HYDROGENASE; NANOSTRUCTURES; POLYMERS; TEMPERATURE; THIOCAPSA ROSEOPERSICINA;

EID: 27544465214     PISSN: 15306984     EISSN: None     Source Type: Journal    
DOI: 10.1021/nl0512224     Document Type: Article

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15. Heat treated crude extracts were prepared by cell lysis by pressure cell treated followed by incubation at 55°C for 10 min, overnight precipitation at 4°C and removal of cellular paniculate and precipitated protein by centrifugation at 20 000g.
16. Tr and Lm hydrogenases are not susceptible to proteolytic digestion.
17. Samples of C. pasteurianum extract were treated with a protease cocktail for a 25 min period prior to activity assay.