Literature DB >> 574862

Effect of succinylation on the oligomeric structure of glycinin.

A G Rao, M S Rao.   

Abstract

By varying the ratio of succinic anhydride to the protein, glycinin, one of the major fractions of soybean proteins, is succinylated to various levels. Sedimentation velocity experiments indicate the dissociation of the protein due to succinylation. Viscosity increases and a blue shift occurs in the absorption spectrum. The rate of proteolysis increases. Both dissociation and denaturation of the protein appear to occur. The effect of syccinylation on glycinin and arachin, the major protein of groundnuts, appears to be different.

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Year:  1979        PMID: 574862     DOI: 10.1111/j.1399-3011.1979.tb01937.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  1 in total

1.  Functional Properties of Rye Prolamin (Secalin) and Their Improvement by Protein Lipophilization through Capric Acid Covalent Binding.

Authors:  Zeinab Qazanfarzadeh; Mahdi Kadivar; Hajar Shekarchizadeh; Raffaele Porta
Journal:  Foods       Date:  2021-03-01
  1 in total

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