title: Thermal and pH stability of "beta-benzyme".
abstract: The thermal and pH stability of "beta-benzyme", an artificial chymotrypsin based on beta-cyclodextrin, has been studied and compared with the stability of real chymotrypsin. Artificial chymotrypsin is vastly superior to real chymotrypsin with regard to both temperature and pH stability. The reasons for this increased stability are discussed.
authors.forename: V T
authors.initials: VT
authors.lastname: D'Souza
authors.forename: X L
authors.initials: XL
authors.lastname: Lu
authors.forename: R D
authors.initials: RD
authors.lastname: Ginger
authors.forename: M L
authors.initials: ML
authors.lastname: Bender
mesh_terms: D002918:Chymotrypsin / Q000378:metabolism*; D003505:Cyclodextrins / Q000378:metabolism*; D003912:Dextrins / Q000378:metabolism*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008956:Models, Chemical; D013213:Starch / Q000378:metabolism*; D013816:Thermodynamics; D047392:beta-Cyclodextrins
chemical_list: D003505:Cyclodextrins; D003912:Dextrins; D047392:beta-Cyclodextrins; D013213:Starch; D002918:Chymotrypsin; C051305:chymotrypsin beta-benzyme; C031215:betadex