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1.
Food Funct ; 9(8): 4135-4142, 2018 Aug 15.
Artículo en Inglés | MEDLINE | ID: mdl-30019729

RESUMEN

In this study, with grass fish bones as the substrate, after flavourzyme treatment, and fermentation with Leuconostoc mesenteroides, a fermentation solution with a high content of soluble calcium was obtained. High performance liquid chromatography and GC-MS analysis indicated that free calcium (11.29 mmol L-1) in the fermentation solution was composed of calcium lactate (3.89 mmol L-1), calcium acetate (6.21 mmol L-1), calcium amino acids and small peptide calcium. Animal experiments show that the fermentation solution of grass fish bones could promote the growth and development of calcium-deficient rats. Complex organic calcium could be well absorbed and utilized by rats so that serum calcium, alkaline phosphatase levels, femur weight and other indicators in calcium-deficient rats could be returned to normal levels. The fermentation solution of grass fish bones can avoid the waste of aquatic proteins and fish bone calcium, and it exhibited high calcium bioavailability. Therefore, the fermentation solution of grass fish bones might be used as a new efficient calcium supplement.


Asunto(s)
Huesos/química , Calcio/farmacocinética , Carpas , Fosfatasa Alcalina , Alimentación Animal/análisis , Animales , Densidad Ósea , Calcio/administración & dosificación , Calcio/sangre , Calcio/química , Dieta/veterinaria , Fermentación , Manipulación de Alimentos , Leuconostoc mesenteroides/fisiología , Masculino , Fósforo/sangre , Distribución Aleatoria , Ratas , Ratas Sprague-Dawley
2.
Food Funct ; 6(6): 1919-27, 2015 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-25965854

RESUMEN

Recently, much attention has been given to improving the antioxidant activity of protein hydrolysates via the Maillard reaction, but little is known about the cellular antioxidant activity of Maillard reaction products (MRPs) from protein hydrolysates. We first investigated chemical characterization and the cellular antioxidant activity of MRPs in a shrimp (Litopenaeus vannamei) by-product protein hydrolysate (SBH)-glucose system at 110 °C for up to 10 h of heating. Solutions of SBH and glucose were also heated alone as controls. The Maillard reaction greatly resulted in the increase of hydroxymethylfurfural (HMF) and browning intensity, high molecular weight fraction, and reduction of the total amino acid in SBH with the heating time, which correlated well with the free radical scavenging activity of MRPs. MRPs had stronger inhibiting effects on oxidative stress of human HepG2 cells than the original SBH, and its cellular antioxidant activity strongly correlated with free radical scavenging activity, but less affected by the browning intensity and HMF level. The caramelization of glucose partially affected the HMF level and free radical scavenging activity of MRPs, but it was not related to the cellular antioxidant activity. The cellular antioxidant activity of MRPs for 5 h of heating time appeared to reach a maximum level, which was mainly due to carbonyl ammonia condensation reaction. In conclusion, the Maillard reaction is a potential method to increase the cellular antioxidant activity of a shrimp by-product protein hydrolysate, but the higher HMF levels and the lower amino acid content in MRPs should also be considered.


Asunto(s)
Antioxidantes/química , Proteínas de Artrópodos/química , Hepatocitos/metabolismo , Estrés Oxidativo , Penaeidae/química , Hidrolisados de Proteína/química , Especies Reactivas de Oxígeno/antagonistas & inhibidores , Animales , Antioxidantes/economía , Antioxidantes/aislamiento & purificación , Antioxidantes/metabolismo , Proteínas de Artrópodos/economía , Proteínas de Artrópodos/aislamiento & purificación , Proteínas de Artrópodos/metabolismo , Supervivencia Celular , China , Proteínas en la Dieta/química , Proteínas en la Dieta/economía , Proteínas en la Dieta/aislamiento & purificación , Proteínas en la Dieta/metabolismo , Suplementos Dietéticos/análisis , Suplementos Dietéticos/economía , Conservantes de Alimentos/química , Conservantes de Alimentos/economía , Conservantes de Alimentos/aislamiento & purificación , Conservantes de Alimentos/metabolismo , Industria de Procesamiento de Alimentos/economía , Furaldehído/análogos & derivados , Furaldehído/análisis , Furaldehído/química , Glucosa/química , Células Hep G2 , Calor , Humanos , Residuos Industriales/análisis , Residuos Industriales/economía , Reacción de Maillard , Peso Molecular , Hidrolisados de Proteína/economía , Especies Reactivas de Oxígeno/metabolismo
3.
Peptides ; 30(6): 1028-33, 2009 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-19463733

RESUMEN

Body wall protein from the sea cucumber (Acaudina molpadioidea) was hydrolyzed sequentially with bromelain and alcalase. The hydrolysate was fractionated into two ranges of molecular weight (PH-I, >2 kDa; PH-II, <2kDa) using an ultrafiltration membrane bioreactor system. The PH-II brought about a high angiotensin I-converting enzyme (ACE) inhibitory activity. An ACE inhibitory peptide was isolated from the PH-II, using the chromatographic methods including gel filtration, ion-exchange chromatography and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was a novel peptide, showing very low similarity to other ACE inhibitory peptide sequences, and was sequenced as MEGAQEAQGD. It was found that the inhibitory activity of the peptide was intensified by 3.5 times from IC(50) 15.9 to IC(50) 4.5 microM after incubation with gastrointestinal proteases. The ACE inhibitory peptide from A. molpadioidea showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR), at a dosage of 3 microM/kg.


Asunto(s)
Inhibidores de la Enzima Convertidora de Angiotensina/aislamiento & purificación , Fragmentos de Péptidos/aislamiento & purificación , Pepinos de Mar/química , Inhibidores de la Enzima Convertidora de Angiotensina/farmacología , Animales , Hidrólisis , Peso Molecular , Fragmentos de Péptidos/farmacología , Peptidil-Dipeptidasa A/metabolismo , Factores de Tiempo
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