title: Thermal stability of alpha-amylase from Aspergillus oryzae entrapped in polyacrylamide gel.
abstract: To determine the suitability as a time-temperature indicator for dielectric pasteurization processes, the thermal stability (50-75 degrees C) of Aspergillus oryzae alpha-amylase immobilized in polyacrylamide gel in phosphate buffer, mashed potatoes, and minced shrimp was examined. Changing the cross-linking agent concentration from 3.3 to 5.3% and adding 2% salt did not markedly affect the thermal stability of the immobilized alpha-amylase. Thermal inactivation was first order, and immobilization generally improved the thermal stability of alpha-amylase. z values of the immobilized system in test food systems were 10.2 degrees C (phosphate buffer), 8.45 degrees C (minced shrimp), and 7.78 degrees C (mashed potatoes).
authors.affiliation: College of Agriculture, Chiangmai University, Chiangmai, Thailand.
authors.forename: Patcharin
authors.initials: P
authors.lastname: Raviyan
authors.forename: Juming
authors.initials: J
authors.lastname: Tang
authors.forename: Barbara A
authors.initials: BA
authors.lastname: Rasco
mesh_terms: D000180:Acrylic Resins; D001236:Aspergillus oryzae / Q000201:enzymology*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006358:Hot Temperature; D007700:Kinetics; D033561:Penaeidae / Q000201:enzymology; D011198:Solanum tuberosum / Q000201:enzymology; D013816:Thermodynamics; D000516:alpha-Amylases / Q000378:metabolism*
chemical_list: D000180:Acrylic Resins; D004800:Enzymes, Immobilized; C016680:polyacrylamide gels; D000516:alpha-Amylases