Literature DB >> 12675592

Macroaffinity ligand-facilitated three-phase partitioning (MLFTPP) of alpha-amylases using a modified alginate.

Kalyani Mondal1, Aparna Sharma, Lata Lata, Munishwar Nath Gupta.   

Abstract

The crude extracts of alpha-amylases when mixed with alginate, tert-butyl alcohol, and ammonium sulfate resulted in an interfacial precipitate containing polymer-bound amylase. The precipitate was dissolved in 1 M maltose to recover alpha-amylase activity. The recovery of alpha-amylases were 74%, 77%, and 92% in the case of Bacillus amyloliquefaciens, wheat germ, and porcine pancreas, respectively. All purified preparations showed a single band on SDS-PAGE.

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Year:  2003        PMID: 12675592     DOI: 10.1021/bp025619e

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  1 in total

1.  Improving Bread Quality with the Application of a Newly Purified Thermostable α-Amylase from Rhizopus oryzae FSIS4.

Authors:  Amel Ait Kaki El-Hadef El-Okki; Mohammed Gagaoua; Hayat Bourekoua; Kahina Hafid; Leila Bennamoun; Shahrazed Djekrif-Dakhmouche; Mohamed El-Hadef El-Okki; Zahia Meraihi
Journal:  Foods       Date:  2017-01-01
  1 in total

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