Effect of oxidation and hydrolysis of porcine myofibrillar protein on N ε ‐carboxymethyl‐lysine formation in model systems

2021 ◽  
Author(s):  
Ligang Yu ◽  
Zhiyong He ◽  
Maomao Zeng ◽  
Yukun Yang ◽  
Jie Chen
Keyword(s):  
Myofibrillar Protein ◽  
Model Systems ◽  
Carboxymethyl Lysine ◽  
Hydrolysis Of

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

1999 ◽  
Vol 65 (8) ◽  
pp. 3540-3546 ◽  
Author(s):  
Silvina Fadda ◽  
Yolanda Sanz ◽  
Graciela Vignolo ◽  
M.-Concepción Aristoy ◽  
Guillermo Oliver ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Myofibrillar Protein ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Whole Cells ◽  
Sarcoplasmic Proteins ◽  
Cell Extracts ◽  
Hydrophobic Nature ◽  
Hydrolysis Of

ABSTRACT Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening,L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.

scholarly journals Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to N∊-carboxymethyl-lysine- and N∊-(1-carboxyethyl)lysine-modified albumin

2002 ◽  
Vol 364 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Naila AHMED ◽  
Ognian K. ARGIROV ◽  
Harjit S. MINHAS ◽  
Carlos A.A. CORDEIRO ◽  
Paul J. THORNALLEY
Keyword(s):  
Advanced Glycation Endproducts ◽  
Advanced Glycation ◽  
Structural Isomers ◽  
Glycation Endproducts ◽  
Assay Procedure ◽  
Carboxymethyl Lysine ◽  
Glycation Process ◽  
First Time ◽  
Hydrolysis Of

Glycation of proteins leads to the formation of early glycation adducts (fructosamine derivatives) and advanced glycation endproducts (AGEs). Formation of AGEs has been linked to the development of cataract, diabetic complications, uraemia, Alzheimer's disease and other disorders. AGEs are a group of compounds of diverse molecular structure and biological function. To characterize AGE-modified proteins used in studies of structural and functional effects of glycation, an assay was developed that surveys the content of early and advanced glycation adducts in proteins. The assay procedure involved enzymic hydrolysis of protein substrate, derivatization of the hydrolysate with 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) and HPLC of the resulting adducts with fluorimetric detection. Structural isomers of methylglyoxal-derived hydroimidazolone, glyoxal-derived hydroimidazolone, 3-deoxyglucosone-derived hydroimidazolone and Nδ-(4-carboxy-4,6-dimethyl-5,6-dihydroxy-1,4,5,6-tetrahydropyrimidin-2-yl)-ornithine (THP) were determined for the first time. AGEs with intrinsic fluorescence (argpyrimidine, pentosidine) were assayed without derivatization. Limits of detection were 2–17pmol and levels of recovery were 50–99%, depending on the analyte. The AQC assay resolved structural and epimeric isomers of methylglyoxal-derived hydroimidazolones and THP. Hydroimidazolones, THP and argpyrimidine were AGEs of short-to-intermediate stability under physiological conditions, with half-lives of 1–2weeks. Their measurement provides further insight into the glycation process. The assay was applied to the characterization of human serum albumin minimally and highly modified by N∊-carboxymethyl-lysine and N∊-(1-carboxyethyl)-lysine.

scholarly journals Formation and Inhibition of Nε-(Carboxymethyl)lysine in Saccharide-Lysine Model Systems during Microwave Heating

Molecules ◽  
2012 ◽  
Vol 17 (11) ◽  
pp. 12758-12770 ◽  
Author(s):  
Lin Li ◽  
Lipeng Han ◽  
Quanyi Fu ◽  
Yuting Li ◽  
Zhili Liang ◽  
...  
Keyword(s):  
Microwave Heating ◽  
Model Systems ◽  
Carboxymethyl Lysine

scholarly journals Insight into the Effects of Sous Vide on Cathepsin B and L Activities, Protein Degradation and the Ultrastructure of Beef

Foods ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1441
Author(s):  
Yantao Yin ◽  
Jailson Pereira ◽  
Lei Zhou ◽  
Jose M. Lorenzo ◽  
Xiaona Tian ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Sarcomere Length ◽  
Cathepsin L ◽  
Myofibrillar Protein ◽  
Potential Mechanism ◽  
Beef Tenderness ◽  
Fragmentation Index ◽  
Sous Vide ◽  
Hydrolysis Of ◽  
Insight Into

This study aimed to evaluate the effects of sous vide cooking (SV) on beef tenderness and its underlying potential mechanism. Beef semimembranosus (SM) were subjected to SV treatments at 45 °C, 55 °C and 65 °C for 4 h. Compared with control samples (CK, cooked at 75 °C until a core temperature of 72 °C was attained), SV treatment significantly promoted the release of cathepsin B and cathepsin L from lysosomes and decreased the shear force of beef SM (p < 0.05). In comparison with CK, samples treated with SV had more hydrolysis of myosin heavy chain and obtained higher myofibrillar fragmentation index, collagen solubility as well as longer sarcomere length (p < 0.05). The current study showed that the proteolysis of myofibrillar protein and collagen induced by cathepsin B and cathepsin L, and the limited longitudinal shrinkage together contributed to the improvement of beef tenderness upon SV.

scholarly journals Multistage Chemical Recycling of Polyurethanes and Dicarbamates: A Glycolysis–Hydrolysis Demonstration

2021 ◽  
Vol 13 (6) ◽  
pp. 3583
Author(s):  
Pegah Zahedifar ◽  
Lukasz Pazdur ◽  
Christophe M.L. Vande Velde ◽  
Pieter Billen
Keyword(s):  
Bottom Layer ◽  
High Potential ◽  
Model Systems ◽  
Production Yield ◽  
Chemical Recycling ◽  
Reaction Conditions ◽  
Material Cycle ◽  
Hydrolysis Of

The use of polyurethanes and, therefore, the quantity of its scrap are increasing. Considering the thermoset characteristic of most polyurethanes, the most circular recycling method is by means of chemical depolymerization, for which glycolysis is finding its way into the industry. The main goal of polyurethane glycolysis is to recover the polyols used, but only limited attempts were made toward recovering the aromatic dicarbamate residues and derivates from the used isocyanates. By the split-phase glycolysis method, the recovered polyols form a top-layer phase and the bottom layer contain transreacted carbamates, excess glycol, amines, urea, and other side products. The hydrolysis of carbamates results in amines and CO2 as the main products. Consequently, the carbamates in the bottom layer of polyurethane split-phase glycolysis can also be hydrolyzed in a separate process, generating amines, which can serve as feedstock for isocyanate production to complete the polyurethane material cycle. In this paper, the full recycling of polyurethanes is reviewed and experimentally studied. As a matter of demonstration, combined glycolysis and hydrolysis led to an amine production yield of about 30% for model systems. With this result, we show the high potential for further research by future optimization of reaction conditions and catalysis.

scholarly journals Enzymatic hydrolysis of grass carp myofibrillar protein and antioxidant properties of hydrolysates

2010 ◽  
Vol 28 (No. 6) ◽  
pp. 475-484 ◽  
Author(s):  
J. Ren ◽  
H. Wang ◽  
M. Zhao ◽  
Ch. Cui ◽  
X. Hu
Keyword(s):  
Grass Carp ◽  
Incubation Temperature ◽  
Antioxidant Activities ◽  
Antioxidant Properties ◽  
Myofibrillar Protein ◽  
Distribution Analysis ◽  
Scavenging Activity ◽  
Inhibitory Effects ◽  
Hydrolysis Of

Myofibrillar protein was extracted from grass carp, a freshwater fish, and hydrolysed using five commercial proteases (papain, pancreatin 6.0, bromelain, Neutrase 1.5MG, and Alcalase 2.4 L). The antioxidant activities of the hydrolysates were determined. Pancreatin 6.0 proved to be the most efficient protease for hydrolysing myofibrillar protein with a very high protein recovery (90.20%), its hydrolysates exhibiting the highest hydroxyl radical (&bull;OH) scavenging activity (IC<sub>50</sub> = 349.89 &plusmn; 11.50 &mu;g/ml) out of all five hydrolysates. Molecular weight distribution analysis revealed that pancreatin 6.0 hydrolysate rendered a higher proportion of the 6&minus;10 kDa fraction and a lower proportion of the 3&minus;6 kDa fraction as compared with other hydrolysates. The maximum &bull;OH scavenging activity for pancreatin 6.0 hydrolysate (IC<sub>50</sub> = 229.90 &micro;g/ml) was obtained at the enzyme to substrate ratio of 0.52%, the incubation time of 7.03 h, and the incubation temperature of 50.56&deg;C, as optimised by response surface methodology. In vitro antioxidant experiments proved that pancreatin 6.0 hydrolysates had obvious inhibitory effects on lipid peroxidation and low-density lipoproteins oxidation under optimised conditions.

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