Literature DB >> 12926898

Thermal stability of alpha-amylase from Aspergillus oryzae entrapped in polyacrylamide gel.

Patcharin Raviyan1, Juming Tang, Barbara A Rasco.   

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).

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Year:  2003        PMID: 12926898     DOI: 10.1021/jf020906j

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  3 in total

1.  Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1.

Authors:  Vimal S Prajapati; Ujjval B Trivedi; Kamlesh C Patel
Journal:  Indian J Microbiol       Date:  2013-04-28       Impact factor: 2.461

2.  Production and biochemical characterization of α-glucosidase from Aspergillus niger ITV-01 isolated from sugar cane bagasse.

Authors:  S Del Moral; D M Barradas-Dermitz; M G Aguilar-Uscanga
Journal:  3 Biotech       Date:  2017-12-11       Impact factor: 2.406

3.  Entrapment of α-Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate.

Authors:  Manu Sharma; Vinay Sharma; Dipak K Majumdar
Journal:  Int Sch Res Notices       Date:  2014-09-15
  3 in total

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