Research in Glycated Progress and Products of Human Serum Albumin by Infrared and CD Spectroscopy

In this study, human serum albumin (HSA) glycated products in dry processing, HSA and glucose were mixed into solution with mass proportion of 1 : 1, free-drying for 48 h, totally 20 samples were obtained according to different reaction times. This study mainly used multi-spectral technology (UV, fluorescence, near infrared spectroscopy, infrared spectroscopy, CD spectroscopy) to analyze the changes of protein secondary tertiary structure, functional groups after glycation of HSA, glycated product and progress of protein. The results show that, the glycation process is easy to occur when HSA was mixed with the glucose in hot and dry conditions, with the increase of reaction time, UV absorption intensity weakened, fluorescence absorption intensity increased and reveal the higher degree of glycation and Maillard reaction, the secondary tertiary structure of protein had small changes. The reaction took about 140 min, the glycation was complete, the Amadori product was formed, and then was further heated to about 240 mm, the reaction entered the middle and late period, and the aldehydes and ketones were formed. The reaction took about 280 min, protein amino groups and carbonyl compounds occurred decarboxylation and deamination.