title: Suppression of α-Amylase inactivation in the presence of ethanol: Application of a two-step model.
abstract: A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca2+) ion dissociates reversibly from the enzyme followed by an irreversible thermal inactivation of the apoenzyme. In this study we report inactivation of the enzyme in the presence of ethanol-water solutions. We noticed that as the concentration of ethanol in the aqueous solution is increased, the thermal inactivation of the enzyme is suppressed with almost no inactivation (in 1 h, 30°C) when 50% alcohol is present in the solution. These results are explained by the two-step inactivation model. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1271-1275, 2016.
authors.affiliation: Dept. of Chemistry, Pennsylvania State University, DuBois, PA, 15801.
authors.forename: Vincent T
authors.initials: VT
authors.lastname: Calabrese
authors.affiliation: Dept. of Chemistry, Pennsylvania State University, DuBois, PA, 15801.
authors.forename: Jason W
authors.initials: JW
authors.lastname: Minns
authors.affiliation: Dept. of Chemistry, Pennsylvania State University, DuBois, PA, 15801. kub@psu.edu.
authors.forename: Arshad
authors.initials: A
authors.lastname: Khan
mesh_terms: D000431:Ethanol / Q000494:pharmacology*; D008954:Models, Biological; D012996:Solutions; D014867:Water / Q000737:chemistry; D000516:alpha-Amylases / Q000037:antagonists & inhibitors* / Q000378:metabolism
chemical_list: D012996:Solutions; D014867:Water; D000431:Ethanol; D000516:alpha-Amylases
keywords: ethanol solutions; heat inactivation; stabilization in nonaqueous solutions; α-amylase