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Updated: Nov 22, 2025
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Structural and antimicrobial properties of Maillard reaction products in chicken liver protein hydrolysate after
Xiao Chen1, Di Jiang2, Pingping Xu2
1Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, PR China; Anhui Engineering Laboratory for Agro-products Processing, Anhui Agricultural University, Hefei, 230036, PR China.
Abstract:
This study aimed to investigate the structural and antimicrobial properties of Maillard reaction products (MRPs) in chicken liver protein (CLP) and its hydrolysate (CLPH) after sonication (SCLPH). The MRPs of CLP (CLPM), CLPH (CLPHM) and SCLPH (SCLPHM) were analyzed by several spectrometric techniques. The molecular weights of the CLPHM and SCLPHM were primarily between 1.35 kDa and 17 kDa. Moreover, the molecular weights in the CLPHM and SCLPHM below 1.35 kDa were increased, which indicated that cross-linking and thermal degradation occurred during the Maillard reaction (MR). The SCLPHM showed an obvious network skeleton, and the surface had many small crystal-shaped particles after ultrasound treatment and MR by scanning electron microscopy. The SCLPHM had more negative charges than the CLPHM, thus effectively inhibiting the growth of S. saprophyticus and E. coli. MR and ultrasound treatment could be a promising technology to expand the application prospects of low-value meat byproducts.
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