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1.
J Sci Food Agric ; 104(6): 3665-3675, 2024 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-38158728

RESUMO

BACKGROUND: The limited physicochemical properties (such as low foaming and emulsifying capacity) of mung bean protein hydrolysate restrict its application in the food industry. Ultrasound treatment could change the structures of protein hydrolysate to accordingly affect its physicochemical properties. The aim of this study was to investigate the effects of ultrasound treatment on the structural and physicochemical properties of mung bean protein hydrolysate of protamex (MBHP). The structural characteristics of MBHP were evaluated using tricine sodium dodecylsulfate-polyacrylamide gel electrophoresis, laser scattering, fluorescence spectrometry, etc. Solubility, fat absorption capacity and foaming, emulsifying and thermal properties were determined to characterize the physicochemical properties of MBHP. RESULTS: MBHP and ultrasonicated-MBHPs (UT-MBHPs) all contained five main bands of 25.8, 12.1, 5.6, 4.8 and 3.9 kDa, illustrating that ultrasound did not change the subunits of MBHP. Ultrasound treatment increased the contents of α-helix, ß-sheet and random coil and enhanced the intrinsic fluorescence intensity of MBHP, but decreased the content of ß-turn, which demonstrated that ultrasound modified the secondary and tertiary structures of MBHP. UT-MBHPs exhibited higher solubility, foaming capacity and emulsifying properties than MBHP, among which MBHP-330 W had the highest solubility (97.32%), foaming capacity (200%), emulsification activity index (306.96 m2 g-1 ) and emulsion stability index (94.80%) at pH 9.0. CONCLUSION: Ultrasound treatment enhanced the physicochemical properties of MBHP, which could broaden its application as a vital ingredient in the food industry. © 2023 Society of Chemical Industry.


Assuntos
Fabaceae , Vigna , Vigna/química , Hidrolisados de Proteína/química , Proteínas de Plantas/química , Solubilidade
2.
Int J Mol Sci ; 23(7)2022 Apr 05.
Artigo em Inglês | MEDLINE | ID: mdl-35409375

RESUMO

Meretrix lusoria (M. lusoria) is an economically important shellfish which is widely distributed in South Eastern Asia that contains bioactive peptides, proteins, and enzymes. In the present study, the extracted meat content of M. lusoria was enzymatic hydrolyzed using four different commercial proteases (neutrase, protamex, alcalase, and flavourzyme). Among the enzymatic hydrolysates, M. lusoria protamex hydrolysate (MLPH) fraction with MW ≤ 1 kDa exhibited the highest free radical scavenging ability. The MLPH fraction was further purified and an amino acid sequence (KDLEL, 617.35 Da) was identified by LC-MS/MS analysis. The purpose of this study was to investigate the anti-obesity and anti-hyperglycemic effects of MLPH containing antioxidant peptides using ob/ob mice. Treatment with MLPH for 6 weeks reduced body and organ weight and ameliorated the effects of hepatic steatosis and epididymal fat, including a constructive effect on hepatic and serum marker parameters. Moreover, hepatic antioxidant enzyme activities were upregulated and impaired glucose tolerance was improved in obese control mice. In addition, MLPH treatment markedly suppressed mRNA expression related to lipogenesis and hyperglycemia through activation of AMPK phosphorylation. These findings suggest that MLPH has anti-obesity and anti-hyperglycemic potential and could be effectively applied as a functional food ingredient or pharmaceutical.


Assuntos
Antioxidantes , Hidrolisados de Proteína , Proteínas Adaptadoras de Transdução de Sinal , Animais , Antioxidantes/química , Antioxidantes/farmacologia , Cromatografia Líquida , Hidrólise , Hipoglicemiantes/farmacologia , Hipoglicemiantes/uso terapêutico , Camundongos , Obesidade/tratamento farmacológico , Peptídeos/química , Peptídeos/farmacologia , Hidrolisados de Proteína/química , Hidrolisados de Proteína/farmacologia , Hidrolisados de Proteína/uso terapêutico , Espectrometria de Massas em Tandem
3.
Metabolites ; 9(9)2019 Sep 12.
Artigo em Inglês | MEDLINE | ID: mdl-31547343

RESUMO

Data on fractionation and depolymerization of the matrix ulvan polysaccharides, and studies on the biological activities on skin cells, are very scarce. In this work, crude ulvans were produced by using EAE (enzyme-assisted extraction) and compared to maceration (an established procedure). After different fractionation procedures-ethanolic precipitation, dialysis, or ammonium sulfate precipitation-the biochemical composition showed that EAE led to an increased content in ulvans. Coupling EAE to sulfate ammonium precipitation led to protein enrichment. Oligosaccharides were obtained by using radical depolymerization by H2O2 and ion-exchange resin depolymerization. Sulfate groups were partially cleaved during these chemical treatments. The potential bioactivity of the fractions was assessed using a lipoxygenase inhibition assay for anti-inflammatory activity and a WST-1 assay for human dermal fibroblast viability and proliferation. All ulvans extracts, poly- and oligosaccharidic fractions from EAE, expanded the fibroblast proliferation rate up to 62%. Our research emphasizes the potential use of poly- and oligosaccharidic fractions of Ulva sp. for further development in cosmetic applications.

4.
PeerJ ; 6: e6181, 2018.
Artigo em Inglês | MEDLINE | ID: mdl-30595992

RESUMO

Pacific chub mackerel (Scomber japonicus) is an important fish throughout the world, especially in East Asian countries, including Korea, China, and Japan. Protein hydrolysates from marine sources are commonly used as nutritional supplements, functional ingredients, and flavor enhancers in the food, beverage, and pharmaceutical industries. Antioxidants isolated from fish are relatively easy to prepare, are cost effective, and have no reported side effects. Hence, the present study aimed to investigate the in vivo antioxidant activities of mackerel muscle protein hydrolysate (MMPH) prepared using Protamex. The in vivo bioactivities of MMPH were investigated in alcoholic fatty liver mice (C57BL/6). Serum alanine aminotransferase and aspartate aminotransferase levels were comparable in test and control mice, whereas serum triglyceride and lipid peroxidation levels significantly (p < 0.05; p < 0.001) decreased after administration of MMPH (100-500 mg kg-1), especially at a concentration of 100 mg kg-1. A significant (p < 0.05) reduction in xanthine oxidase activity was observed in all groups treated with MMPH (100-500 mg kg-1), as compared with the control group. Significantly (p < 0.05) higher superoxide dismutase (SOD) activity/protein expression and regulated catalase (CAT) activity/protein expression levels were observed in groups administered MMPH (100-500 mg kg-1), especially at a concentration of 100 mg kg-1. These results show that the abundant amino acids of S. japonicus play an important role in the cytosol of the liver cells by directly participating in the expression of xanthine oxidase and the detoxifying SOD and CAT proteins, thereby enhancing antioxidant ability and ultimately, inhibiting lipid peroxidation. This study demonstrated that muscle protein hydrolysate from S. japonicus has strong antioxidant activities.

5.
Food Chem ; 187: 270-8, 2015 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-25977026

RESUMO

Protamex catalyzed corn gluten meal (CGM) hydrolysis peptides (CHP) were prepared. Orthogonal design L16 (4(5)) was used to optimize processing variables of CGM concentration, CGM heat pretreatment (121 °C) time, and enzymolysis pH, temperature, and time. Degree of hydrolysis (DH), undigested residue ratio, molecular weight (MW) distribution and DPPH radical inhibition were selected as analysis indicators. Optimum variables were CGM concentration of 18%, heat pretreatment time of 40 min, and enzymolysis pH, temperature and time of 7.5, 55 °C and 24h, respectively. Verification test showed that CHP IC50 for scavenging hydroxyl radical was the best and then followed by reducing power. Oligopeptides improved after hydrolysis at the expense of di- and tripeptides, suggesting formation of soluble aggregates from low MW peptides. The increase in the DH, oligopeptides, Alanyl-Tyrosine, and antioxidant free amino acids coincided with the improvement in the antioxidant activity of CHP.


Assuntos
Antioxidantes/química , Glutens/química , Zea mays/química , Aminoácidos/análise , Dipeptídeos/análise , Análise de Alimentos , Temperatura Alta , Concentração de Íons de Hidrogênio , Hidrólise , Radical Hidroxila/química , Concentração Inibidora 50 , Peso Molecular , Oligopeptídeos/química
6.
Food Chem ; 172: 407-15, 2015 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-25442571

RESUMO

The physicochemical and functional properties, such as surface hydrophobicity, disulphide bond content, thermal properties, molecular weight distribution, antioxidant properties, of corn glutelin hydrolysates catalysed by Protamex at different hydrolysis times were evaluated. The hydrolysis influenced the properties of corn glutelin significantly, and not only decreased its molecular weight and disulphide bond content, but also eventually transformed its insoluble native aggregates to soluble aggregates during the hydrolysis process. Corn glutelin hydrolysates were found to have a higher solubility, which was associated with their relatively higher foaming and emulsifying properties compared to the original glutelin. Corn glutelin and its hydrolysates maintained a high thermal stability. In addition, the hydrolysates exhibited excellent antioxidant properties measured through in vitro assays, namely DPPH and OH radical scavenging activity, Fe(2+)-chelating capacity and reducing power; the values were 58.86%, 82.64%, 29.92% and 0.236% at 2.0mg/mL, respectively.


Assuntos
Glutens/metabolismo , Aminoácidos/análise , Animais , Antioxidantes/química , Varredura Diferencial de Calorimetria , Cromatografia Líquida de Alta Pressão , Cromatografia por Troca Iônica , Dissulfetos/análise , Emulsificantes/química , Glutens/química , Hidrólise , Interações Hidrofóbicas e Hidrofílicas , Peso Molecular , Solubilidade , Fatores de Tempo , Zea mays/metabolismo
7.
Food Res Int ; 75: 123-130, 2015 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-28454938

RESUMO

Bee pollen possesses a broad range of potential biological activities, but nutrient absorption and biological activities of bee pollen may be restricted due to complex pollen wall. This study aimed to investigate wall-disruption variations of Brassica campestris L. (rape) bee pollen treated with protamex hydrolysis, ultrasonication, and combination of protamex hydrolysis and ultrasonication. Pollen sample treated with these three treatments had higher specific surface area values and smaller particle sizes than the untreated sample. Protamex hydrolysis degraded the pollen coat and disintegrated the intine at the germinal apertures. Ultrasonication treatment cracked the pollen exine into fragments, but seemed to have little effect on the intine. The combination of protamex hydrolysis and ultrasonication can degrade pollen coat and entirely disrupt both the exine and the intine. The exine of rape bee pollen was disrupted into three fragments along germinal apertures.

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