Mechanochemically Induced Controlled Glycation of Lysozyme and Its Effect on Enzymatic Activity and Conformational Changes

Journal of Agricultural and Food Chemistry
Haoran Xing, Varoujan A Yaylayan

Abstract

Protein glycation through heating of a mixture of protein and reducing sugars is one of the most commonly used methods of protein modification; however, in most cases, this approach can lead to uncontrolled glycation. The hypothesis that mechanical energy supplied through ball milling can induce glycation of proteins was tested using a well-characterized enzyme lysozyme. The Q-TOF/MS analysis of the milled samples has indicated that the milling of sugar-protein mixtures in stainless steel jars for 30 min and at a frequency of 30 Hz generated mainly monoglycated proteins even with the highly reactive ribose. Increasing the sugar concentration or the milling time did not influence the overall yield or generate more glycoforms. Enzymatic activity measurements, FTIR, and fluorescence spectroscopic studies have indicated that milling of lysozyme alone leads to a significant loss in enzymatic activity and structural integrity in contrast to milling in the presence of sugars.

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Feb 27, 2018·Carbohydrate Research·Haoran Xing, Varoujan A Yaylayan

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Citations

Oct 28, 2019·Chembiochem : a European Journal of Chemical Biology·Sandra KaabelKarine Auclair
Sep 29, 2020·Journal of Chemical Information and Modeling·Daisuke MiyataShin-Ichi Morita

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