Extraction and characterization of novel multifunctional peptides from Trachinus Draco (greater weever) myofibrillar proteins with ACE/DPP4 inhibitory, antioxidant, and metal chelating activities

2020 ◽  
Vol 44 (5) ◽  
Author(s):  
Elif Kula ◽  
Ebru Kocadag Kocazorbaz ◽  
Hichem Moulahoum ◽  
Senol Alpat ◽  
Figen Zihnioglu
Keyword(s):  
Myofibrillar Proteins ◽  
Metal Chelating ◽  
Multifunctional Peptides

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.

Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease

2009 ◽  
Vol 131 (4) ◽  
pp. 1436-1451 ◽  
Author(s):  
Cristina Rodríguez-Rodríguez ◽  
Natalia Sánchez de Groot ◽  
Albert Rimola ◽  
Ángel Álvarez-Larena ◽  
Vega Lloveras ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Intercalation Compounds ◽  
Metal Chelating ◽  
Design Selection

scholarly journals Characterization of Mussel Inspired Surface Modified and Metal Chelated Polymer Membrane

2020 ◽  
Vol 9 (3) ◽  
pp. 2847-2852
Keyword(s):  
Polyvinylidene Fluoride ◽  
Membrane Surface ◽  
Chelating Agent ◽  
Flux Analysis ◽  
Permeate Flux ◽  
Functional Protein ◽  
Metal Chelating ◽  
Coating Absorption ◽  
Surface Modified

Modification of a membrane surface is critical to help further functional protein binding on the membrane. Mussel inspired modification and metal chelating agent grafting on the polyvinylidene fluoride (PVDF) is proposed to increase the hydrophilicity, stability, and functionality of the membrane. This study carried out a four steps modification including polymerization of dopamine, grafting with poly (ethyleneimine) (PEI) and metal chelating agent and finally metal (ZnO) coupling. Characterization of the modified membrane was carried out using contact angle observation, permeate flux analysis, FT-IR spectrum and FESEM analysis. The results show a successful PDA and PEI deposition on PVDF membrane with significant improvement of the membrane hydrophilicity and wettability. Permeate flux analysis showed blockage on membrane surface due to the successful coating. Absorption peak increased slightly showing the deposition of PDA/PEI. Successful Zn2+ ion coupling can be seen clearly from the FESEM analysis

Characterization of healthier mixed surimi gels obtained through partial substitution of myofibrillar proteins by pea protein isolates

2020 ◽  
Vol 107 ◽  
pp. 105976 ◽  
Author(s):  
A. Javier Borderías ◽  
Clara A. Tovar ◽  
Fátima Domínguez-Timón ◽  
M. Teresa Díaz ◽  
Mercedes M. Pedrosa ◽  
...  
Keyword(s):  
Partial Substitution ◽  
Myofibrillar Proteins ◽  
Protein Isolates ◽  
Pea Protein

Expression and Characterization of Recombinant Drosophila 6-pyruvoyl tetrahydropterin Synthase

Pteridines ◽  
1995 ◽  
Vol 6 (2) ◽  
pp. 58-62
Author(s):  
Young Shik Park ◽  
Nacksung Kim ◽  
Hajeong Kim ◽  
Dongkook Park ◽  
Jeongbin Yim
Keyword(s):  
Recombinant Protein ◽  
Isoelectric Point ◽  
Crude Extract ◽  
Fusion Proteins ◽  
Heat Stability ◽  
Native Enzyme ◽  
Metal Chelation ◽  
E Coli ◽  
Metal Chelating

Summary 6-Pyruvoyl tetrahydropterin synthase is involved in the synthesis of pteridine eye pigments in Drosophila. The purple gene which was known to be one of the target loci of the suppressor mutation su(sj2 has been identified to encode the enzyme, and its cDNA has been cloned recently. The cDNA encoding the 19.3 kDa subunit of the 6-pyruvoyl tetrahydropterin synthase was expressed as fusion proteins in E. coli. The recombinant protein was shown to be active and purified from the E. coli crude extract by metal-chelation chromatography. The fused metal-chelating oilgopeptide was removed by thrombin for further characterization. Apparent Km for the substrate dihydroneopterin triphosphate was determined to be 590 IlM, which was slightly higher than the value of the native enzyme. The isoelectric point of 6.4 was also different from the known value of 4.3 determined by the native enzyme. Heat stability and the stimulatory effect of reducing agents were similar to the native enzyme. The modification of cysteine residues in the recombinant enzyme, one of which is known to be conserved in human and rat enzymes, by iodoacetamide inhibited its activity by up to 80%.

Characterization of a Metal-Chelating Substance in Coffee

2005 ◽  
Vol 69 (1) ◽  
pp. 26-30 ◽  
Author(s):  
Makiko TAKENAKA ◽  
Naoko SATO ◽  
Hiromi ASAKAWA ◽  
Xu WEN ◽  
Masatsune MURATA ◽  
...  
Keyword(s):  
Metal Chelating

Chemical characterization of the glycated myofibrillar proteins from grass carp (Ctenopharyngodon idella) and their impacts on the human gut microbiota in vitro fermentation

2017 ◽  
Vol 8 (3) ◽  
pp. 1184-1194 ◽  
Author(s):  
Kaining Han ◽  
Ye Yao ◽  
Shiyuan Dong ◽  
Sun Jin ◽  
Hang Xiao ◽  
...  
Keyword(s):  
Grass Carp ◽  
Chemical Characterization ◽  
Ctenopharyngodon Idella ◽  
Myofibrillar Proteins ◽  
Human Gut ◽  
In Vitro Fermentation ◽  
Microbial Community Structures ◽  
Grass Carp Ctenopharyngodon Idella

Glycation greatly increased the anti-digestibility of myofibrillar proteins derived from grass carp, and affected the production of SCFAs and the microbial community structures inin vitrofecal fermentation.

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