, Volume 46, Issue 3, pp 251-255
Date: 27 Feb 2010

The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum

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Biological context

Protein deamidation, the hydrolysis of side chain amido groups of protein-bound glutaminyl or asparaginyl residues to release ammonia, has received focused attention especially in food industries since protein deamidation is regarded as a promising method to improve functional properties of food proteins. Deamidation generally decreases an isoelectric point of proteins due to increase in number of negatively charged carboxyl groups and enhances protein solubility. In addition, deamidation leads to alteration of the tertiary structures of proteins with an improved amphiphilic character that is useful as an emulsifier or a foaming agent. Therefore, deamidation of food proteins have been investigated by various methods including mild acid treatment, anion-catalyzed deamidation, dry heating under mild alkaline conditions, and thermal treatment. Although deamidation by these treatments improved protein functionalities, there were undesired side-effects, such as concomitant...