Formation of advanced glycation endproducts in ground beef under pasteurisation conditions

Sun, Xiangming; Tang, Juming; Wang, Jing; Rasco, Barbara; Lai, Keqiang; Huang, Yiqun

doi:10.1016/j.foodchem.2014.09.129

Cited by 102 publications

(66 citation statements)

References 23 publications

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“…Recovery experiments were conducted by spiking samples with 0.25, 0.6, and 1.2 ng/μl of CML ( n = 3), for which the recovery rates were 79.8 ± 14.9%, 80.5 ± 9.0%, and 88.9 ± 4.5%, respectively. The recovery and linearity of CML in some previous reports compared favorably with our study (Sun et al., ; Zhang, Huang, Xiao, & Mitchell, ).…”

Section: Resultssupporting

confidence: 90%

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

2018

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Background and objectives The adverse health effects of advanced glycation endproducts (AGEs) is of current interest; some previous research indicates that consuming these compounds may contribute to chronic diseases such as diabetes and heart disease. The objective of this study was to determine whether cereal bran extract from wheat (Jagger, JA), triticale (Spring Triticale, ST, and Thundercale, TH), and Rye (RY) can inhibit the formation of AGE in a bovine serum albumin/glucose (BSA/GLU) model. Findings Nε‐carboxymethyllysine (CML) levels showed ST extract inhibited AGE formation, but TH, RY, and JA extracts did not affect AGE formation in the BSA/GLU system. Subsequent HPLC analysis of ST extract revealed four major phenolic acids: vanillic (VA), chlorogenic (CHA), gentisic (GEA), and ferulic (FA). The results also showed antioxidant and antiglycation properties of these phenolic acids. Conclusions GEA and CHA in ST extract were effective free radical scavengers and acted against dicarbonyl compounds. Significance and novelty ST bran extract may be considered as a natural source of inhibitors of in vitro formation of AGEs.

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Section: Resultssupporting

confidence: 90%

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

2018

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“…The Maillard reaction can occur upon heating of meat because meat contains a small amount of carbohydrates, primarily those originating from glycogen and nucleotides (Schmidt ). The formation of 2 common AGEs, N ε ‐carboxymethyllysine (CML) and N ε ‐carboxyethyllysine (CEL), has been characterized in ground beef under pasteurization conditions covering wide ranges of heating temperatures (65 to 100 °C) and heating times (0 to 60 min) (Sun and others ). The AGEs were released by acid hydrolysis and analyzed by hydrophilic interaction LC‐MS/MS operated in multiple reaction monitoring (MRM) mode.…”

Section: Amino Acid Residue‐level Modifications After Heatingmentioning

confidence: 99%

Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

175

115

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Food ingredients commonly undergo heat treatment. Meat, in particular, is typically consumed after some form of heating, such as boiling or roasting. Heating of meat can introduce a wide range of structural changes in its proteinaceous components. At the 3-dimensional structural level, meat proteins may denature and form aggregates upon heating. At the molecular level, primary structure (amino acid residue) alterations reported in cooked meat include protein carbonylation, modification of aromatic residues, and the formation of Maillard reaction products. Identification of these modifications is essential for determining the mechanism of thermal processing of meat and allowing better control of the nutritional and functional properties of products. This article reviews and summarizes the current state of understanding of protein modifications at the molecular level in commonly consumed mammalian food. In addition, relevant case studies relating to characterization of heat-induced amino acid residue-level modifications in other biological materials such as milk and wool are discussed to provide complementary insights.

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“…0.2‐g meat (with an error of 0.001 g) was accurately weighed and put into a 50‐ml centrifuge tube. The protein‐binding CML and CEL were determined by Sun's method with some modifications (Sun et al, ). Samples were put under the condition of 4℃ by adding sodium borate buffer solution and sodium borohydride solution to reduction for a night.…”

Section: Methodsmentioning

confidence: 99%

“…There are many factors influencing the formation of CML and CEL; two common factors are thermal processing conditions and the levels of precursor substances such as protein, fat, and water (Sun et al, ). Processing temperature has a significant effect on the formation of AGEs.…”

Section: Introductionmentioning

confidence: 99%

Content of free and protein‐binding N^ε‐carboxymethyllysine and N^ε‐carboxyethyllysine in different parts of braised chicken

Zhu

Fang

Cheng

et al. 2020

Food Science & Nutrition

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In order to illustrate the levels of advanced glycation end products (AGEs) in Chinese traditional braised chicken, the distribution of free and protein‐binding Nε‐carboxymethyllysine (CML) and Nε‐carboxyethyllysine (CEL) in four parts of processed chicken including chest (X), leg (T), skin (P), and the mixed whole body (M) was investigated. Our results showed that the content of free CML was 1,186.63–1,795.43 ng/g meat and protein‐binding CML was 11,693.91–16,122.90 ng/g meat. Differently, the content of free CEL was 24.81–41.62 ng/g meat and protein‐binding CEL was 270.11–385.49 ng/g meat. It was found that the total contents of CML were 31.5–56.8 folds higher than those of CEL. Protein‐binding AGEs (CML + CEL) were 6.6–9.9 times higher than those of free AGEs (CML + CEL). Pearson's correlation of AGEs and oxidation in four parts of braised chicken were also investigated, and the results showed that oxidation had a significant effect on levels of CEL; especially, the protein carbonyl was negatively correlated with free CEL (p < .05). TBARs value was significantly positively correlated with protein‐binding and total CEL (p < .01). In conclusion, our findings are important for better understanding of the AGEs formation in braised meat.

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Formation of advanced glycation endproducts in ground beef under pasteurisation conditions

Cited by 102 publications

References 23 publications

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

Cooking‐Induced Protein Modifications in Meat

Content of free and protein‐binding N^ε‐carboxymethyllysine and N^ε‐carboxyethyllysine in different parts of braised chicken

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Formation of advanced glycation endproducts in ground beef under pasteurisation conditions

Cited by 102 publications

References 23 publications

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

Cereal bran extracts inhibit the formation of advanced glycation endproducts in a bovine serum albumin/glucose model

Cooking‐Induced Protein Modifications in Meat

Content of free and protein‐binding Nε‐carboxymethyllysine and Nε‐carboxyethyllysine in different parts of braised chicken

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Content of free and protein‐binding N^ε‐carboxymethyllysine and N^ε‐carboxyethyllysine in different parts of braised chicken