Comparison of two kinds of peroxyl radical pretreatment at chicken myofibrillar proteins glycation on the formation of Nε-carboxymethyllysine and Nε-carboxyethyllysine

This publication has 40 references indexed in Scilit:

• Effects of raw meat and process procedure on Nε-carboxymethyllysine and Nε-carboxyethyl-lysine formation in meat products
  Food Science and Biotechnology, 2016
• Effects of oxidised linoleic acid on the formation of N^ε‐carboxymethyl‐lysine and N^ε‐carboxyethyl‐lysine in Maillard reaction system
  International Journal of Food Science and Technology, 2015
• Influence of linoleic acid-induced oxidative modifications on physicochemical changes and in vitro digestibility of porcine myofibrillar proteins
  LWT, 2015
• Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals
  Meat Science, 2014
• Glyoxal derived from triglyceride participating in diet-derived Nε-carboxymethyllysine formation
  Food Research International, 2013
• Hydroxyl Radical and Ferryl‐Generating Systems Promote Gel Network Formation of Myofibrillar Protein
  Journal of Food Science, 2010
• Microstructure–function relationships of heat-induced gels of porcine haemoglobin
  Food Hydrocolloids, 2009
• Variation in the Cross-Linking Pattern of Porcine Myofibrillar Protein Exposed to Three Oxidative Environments
  Journal of Agricultural and Food Chemistry, 2008
• Oxidation of Free Tryptophan and Tryptophan Residues in Peptides and Proteins
  Journal of Agricultural and Food Chemistry, 1998
• Estimation of disulfide bonds using 2-nitro-5-thiosulfobenzoic acid: Limitations
  Analytical Biochemistry, 1985