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RISS 인기검색어
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- 저자 : Maria Teresa Bertoldo Pacheco (검색결과 2 건)
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Effect of Different Hydrolysates of Whey Protein on Hepatic Glutathione Content in Mice
Maria Teresa Bertoldo Pacheco,Valdemiro Carlos Sgarbieri 한국식품영양과학회 2005 Journal of medicinal food Vol.8 No.3
This study was designed to compare the effects of diets prepared with enzymatic hydrolysate of a whey pro-tein concentrate (WPC) by pancreatin, protamex™ (Novo Nordisk, Bagsvaerd, Denmark), and alcalase proteases on the he-patic glutathione content in mice. The undenatured WPC was produced in a pilot plant by membrane technology (microfil-tration/diafiltration) after separation of the casein clot through a conventional process. All three hydrolysates with 20% degreeof hydrolysis showed an amino acid profile similar to WPC. Male A/J mice were fed on diets containing 20% WPC or hy-drolysates. Commercial casein was used as a reference protein in the biological assays. The glutathione content was deter-mined after liver extraction through high-performance capillary electrophoresis. WPC and its pancreatin and protamex hy-drolysates showed higher ability to stimulate liver glutathione synthesis than alcalase hydrolysate. This difference was probablyrelated to an amino acid sequence in the peptides that were formed during hydrolysis of whey proteins. Commercial caseinand WPC alcalase hydrolysate produced lower stimulation of liver glutathione synthesis (7.09 and 5.66 .mol/g of wet weight)compared with WPC and pancreatin and protamex hydrolysates (8.72, 8.71, and 8.45 .mol/g of wet weight, respectively).These results indicate that the hydrolysates obtained by treatment with pancreatin and protamex are good sources of peptideswith activity to stimulate glutathione synthesis.
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Taliana Kenia Alencar Bezerra,Jose´ Thalles Jocelino Gomes de Lacerda,Bruno Ramos Salu,Maria Luiza Vilela Oliva,Maria Aparecida Juliano,Maria Teresa Bertoldo Pacheco,Marta Suely Madruga 한국식품영양과학회 2019 Journal of medicinal food Vol.22 No.12
Peptides from protein hydrolysate of a mixture of chicken combs and wattles (CCWs) were obtained through enzymatic hydrolysis, and their anticoagulant and inhibitory effects on angiotensin I-converting enzyme (ACE) were investigated. The protein hydrolysate exhibited anticoagulant capacity by the intrinsic pathway (activated partial thromboplastin time) and potent ACE-inhibitory activity. The peptides were sequenced by LC-MS to identify those with higher inhibitory potential. From the pool of sequenced peptides, the following three peptides were selected and synthesized based on their low molecular weight and the presence of amino acids with ACE-inhibitory potential at the C-terminus: peptide I (APGLPGPR), peptide II (Piro-GPPGPT), and peptide III (FPGPPGP). Peptide III (FPGPPGP) showed the highest ACE-inhibitory capacity among the peptides selected. In conclusion, a peptide (FPGPPGP) of unknown sequence was identified as having potent ACE-inhibitory capacity. This peptide originated from unconventional hydrolysates from poultry slaughter waste, including combs and wattles.
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