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1.
Molecules ; 26(19)2021 Sep 27.
Article in English | MEDLINE | ID: mdl-34641397

ABSTRACT

In this study, phenolic compounds from an aqueous protein by-product from rapeseed meal (RSM) were identified by HPLC-DAD and HPLC-ESI-MS, including sinapine, sinapic acid, sinapoyl glucose, and 1,2-di-sinapoyl gentibiose. The main phenolic compound in this by-product was sinapine. We also performed acid hydrolysis to convert sinapine, and sinapic acid derivatives present in the permeate, to sinapic acid. The adsorption of phenolic compounds was investigated using five macroporous resins, including XAD4, XAD7, XAD16, XAD1180, and HP20. Among them, XAD16 showed the highest total phenolic contents adsorption capacities. The adsorption behavior of phenolic compounds was described by pseudo-second-order and Langmuir models. Moreover, thermodynamics tests demonstrated that the adsorption process of phenolic compounds was exothermic and spontaneous. The highest desorption ratio was obtained with 30% (v/v) and 70% (v/v) ethanol for sinapine and sinapic acid, respectively, with a desorption ratio of 63.19 ± 0.03% and 94.68 ± 0.013%. DPPH and ABTS tests revealed that the antioxidant activity of the hydrolyzed fraction was higher than the non-hydrolyzed fraction and higher than the one of vitamin C. Antioxidant tests demonstrated that these phenolic compounds could be used as natural antioxidants, which can be applied in the food industry.


Subject(s)
Antioxidants/pharmacology , Brassica napus/chemistry , Dietary Proteins/isolation & purification , Phenols/pharmacology , Plant Extracts/pharmacology , Plant Proteins/isolation & purification , Resins, Plant/chemistry , Food Handling
2.
J Food Sci ; 86(6): 2539-2552, 2021 Jun.
Article in English | MEDLINE | ID: mdl-34009639

ABSTRACT

This study investigated the effect of pulsed electric fields (PEF) pretreatment on rehydration kinetics, firmness, and release of intracellular components of dried chickpeas during rehydration at 35 to 65°C. After soaking preconditioning, chickpeas were subjected to PEF treatments (2.5 and 3.3 kV/cm, 0.2 to 12.0 kJ/kg, 15 µs pulse width, 20 Hz frequency). PEF treated and untreated chickpeas were dried in crossflow air dryer and their rehydration at constant seed/water ratio of 1:5 was studied for 24 hr. During rehydration, moisture, firmness, and concentration of released proteins, carbohydrates and raffinose family oligosaccharides (RFO) were determined and described using appropriate mathematical models. PEF treatment led to up to 70% higher rehydration rates of dried chickpeas. This increase corresponds to rehydration time of approximately 1.5 hr, as opposed to 5 hr for untreated samples. Firmness of PEF treated chickpeas (for energy inputs higher than 3 kJ/kg) during rehydration decreased up to 30% compared to untreated samples. The firmness of untreated samples after 300 min of rehydration was achieved at much shorter times (up to 30 min) for PEF treated samples. At the end of 300 min of rehydration, more than 47.7%, 76.1%, and 86.6% of total raffinose, stachyose, and verbascose, respectively has been extracted, but only 0.03% of nutritionally valuable proteins from PEF treated chickpeas. Consequently, this study demonstrates that PEF processing could be implemented in dried chickpeas processing as pretreatment, for the reduction of rehydration time prior to cooking and of intestinal discomfort caused by RFO.


Subject(s)
Cicer/chemistry , Cicer/metabolism , Cooking/methods , Dietary Carbohydrates/analysis , Dietary Proteins/analysis , Fluid Therapy/methods , Raffinose/analysis , Dietary Carbohydrates/isolation & purification , Dietary Proteins/isolation & purification , Electricity , Kinetics , Raffinose/isolation & purification
3.
Mar Drugs ; 18(8)2020 Jul 27.
Article in English | MEDLINE | ID: mdl-32727001

ABSTRACT

The global demand for dietary proteins and protein-derived products are projected to dramatically increase which cannot be met using traditional protein sources. Seafood processing by-products (SPBs) and microalgae are promising resources that can fill the demand gap for proteins and protein derivatives. Globally, 32 million tonnes of SPBs are estimated to be produced annually which represents an inexpensive resource for protein recovery while technical advantages in microalgal biomass production would yield secure protein supplies with minimal competition for arable land and freshwater resources. Moreover, these biomaterials are a rich source of proteins with high nutritional quality while protein hydrolysates and biopeptides derived from these marine proteins possess several useful bioactivities for commercial applications in multiple industries. Efficient utilisation of these marine biomaterials for protein recovery would not only supplement global demand and save natural bioresources but would also successfully address the financial and environmental burdens of biowaste, paving the way for greener production and a circular economy. This comprehensive review analyses the potential of using SPBs and microalgae for protein recovery and production critically assessing the feasibility of current and emerging technologies used for the process development. Nutritional quality, functionalities, and bioactivities of the extracted proteins and derived products together with their potential applications for commercial product development are also systematically summarised and discussed.


Subject(s)
Dietary Proteins/metabolism , Dietary Supplements , Industrial Waste , Microalgae/metabolism , Proteins/therapeutic use , Seafood , Animals , Dietary Proteins/chemistry , Dietary Proteins/isolation & purification , Food Handling , Humans , Nutritive Value , Proteins/chemistry , Proteins/isolation & purification
4.
J Nutr Sci Vitaminol (Tokyo) ; 65(Supplement): S148-S152, 2019.
Article in English | MEDLINE | ID: mdl-31619617

ABSTRACT

Dietary therapy through a low-protein diet (LPD) has long been used for preserving the renal function of patients with chronic kidney disease (CKD). Reducing the amount of protein ingested from rice would make it possible to allocate the difference to side dishes, thereby improving the quality of meals and facilitating adherence to LPD. If it is possible to remove protein from rice, it would minimize the need to cut down on main dishes and make it easier for patients to follow the LPD. We developed exclusive technology for digesting and removing protein from rice grain using microorganism-derived enzyme product, and technology for processing the Low-Protein Rice (LPR) thus obtained into a palatable food product. By combining these technologies, we can reliably manufacture delicious, high quality, low protein rice product, which can be eaten repeatedly as staple. Our LPR products, "PLC Rice" series are helpful to enhance the quality of mealtimes for CKD patients by increasing their range of food choices. It is therefore reasonable to say that PLC Rice products offer high added value, as it not only facilitates adhesion to LPD but also add satisfaction and contentment to daily meals, helping to enhance the quality of life of patients with CKD.


Subject(s)
Diet, Protein-Restricted/methods , Dietary Proteins/isolation & purification , Food Handling/methods , Food Technology/methods , Oryza/chemistry , Humans , Renal Insufficiency, Chronic/diet therapy
5.
Food Res Int ; 116: 697-706, 2019 02.
Article in English | MEDLINE | ID: mdl-30716997

ABSTRACT

In our research soluble proteins from edible grasshopper (S. gregaria) and honey bee brood (A. mellifera) were exposed to defatting, alkaline, and sonication-assisted extractions. New nitrogen-to-protein conversion factors based on amino acid analysis were estimated for both insects: 4.5 for adult grasshopper, and 4.9 and 5.6 for pupae and larvae of honey bee respectively, in contrary to 6.25 commonly used for insects. All fractions were characterized by their composition, yield, color, protein solubility, and functional properties in comparison to whey protein concentrate. Besides an increase in protein content up to 57.5 and 55.2% for grasshopper and honey bee respectively, protein-enriched fractions showed improved foaming and emulsifying abilities. The highest emulsion stability after 120 min was determined for grasshopper powder extracted with sonication (85.5%) and whey proteins (89.8%). The protein-enriched fractions of both insects had significantly higher foaming stability (74.1% for grasshopper fraction after alkaline extraction and 55.5% for sonication-assisted honey bee fraction) than raw and defatted powder. All fractions obtained from honey bee brood showed significantly higher protein heat coagulation than grasshopper and whey proteins. Changes in protein functionality were found related to alteration in protein charge, surface hydrophobicity, and distribution of proteins according to their molecular weight. Therefore, our results showed that S. gregaria and A. mellifera have a potential for future applications for food, feed, or insect-based dietary supplements.


Subject(s)
Bees/chemistry , Dietary Proteins/isolation & purification , Grasshoppers/chemistry , Insect Proteins/isolation & purification , Amino Acid Sequence , Animals , Color , Food Handling , Hot Temperature , Hydrophobic and Hydrophilic Interactions , Protein Denaturation , Protein Stability , Solubility , Surface Properties , Whey Proteins/chemistry
6.
Food Chem ; 272: 165-173, 2019 Jan 30.
Article in English | MEDLINE | ID: mdl-30309527

ABSTRACT

Alkali extraction and acid precipitation methods were adopted to isolate protein from quinoa and album seeds of variety Chenopodium. Different pH dispersions (3-11) of isolated proteins were prepared and effects of pH and holding time on protein characteristics were evaluated. The pH-10 of extraction medium was found suitable for protein extraction on the basis of yield, purity, solubility and colour having isoelectric pH of 4.5. Yield and purity of protein isolates (PI) of quinoa and album varied from 8.12 to 12.22%; 74.19 to 85.07% and 7.71 to 10.98%; 77.16 to 86.12%, respectively. Overall, pH and time had significant effect on functional properties of PI of both seeds. Quinoa PI had higher emulsifying activity, emulsion stability, water binding capacity and dispersibility, whereas, foaming capacity and stability were higher for album PI. Nutritional indices were 64.20 and 64.58 for quinoa and album PI, respectively, whereas, amino acid scoring (FAO, 2013) indicated, isoleucine, leucine and valine as the limiting amino acids.


Subject(s)
Amino Acids/analysis , Chemical Fractionation/methods , Chenopodium/chemistry , Plant Proteins/chemistry , Seeds/chemistry , Dietary Proteins/chemistry , Dietary Proteins/isolation & purification , Hydrogen-Ion Concentration , Plant Proteins/isolation & purification , Solubility , Time Factors
7.
Sci China Life Sci ; 61(11): 1396-1406, 2018 Nov.
Article in English | MEDLINE | ID: mdl-30099706

ABSTRACT

This study aimed to explore the rule of degradation of dietary proteins by identifying chyme proteins in different segments of the digestive tract of growing pigs, using proteomics techniques. Six growing pigs were fed a corn-soybean meal-based diet for 7 days. The feedstuff and chyme proteins were separately extracted and separated with SDS-PAGE. 2D LCMS/MS combined with protein database searching identified 1,513 proteins in different segments of the gastrointestinal tract, the number of identified exogenous proteins gradually decline from the stomach to colon, with large amounts in the duodenum to the large intestine. More corn proteins than soybean proteins were identified both in the feedstuff and chyme, and these were significantly decreased after digestion in the stomach. More membrane proteins than non-membrane proteins were identified in whole digestive tract. These results regarding the profiles of chyme proteins in different segments of the gastrointestinal tract would provide useful information for optimizing feed formula in pigs.


Subject(s)
Dietary Proteins/isolation & purification , Gastrointestinal Contents/chemistry , Gastrointestinal Tract/metabolism , Swine/metabolism , Animal Feed/analysis , Animal Nutritional Physiological Phenomena , Animals , Diet/veterinary , Dietary Proteins/analysis , Dietary Proteins/metabolism , Glycine max/chemistry , Glycine max/metabolism , Zea mays/chemistry , Zea mays/metabolism
8.
J Nutr ; 148(8): 1229-1235, 2018 08 01.
Article in English | MEDLINE | ID: mdl-29939292

ABSTRACT

Background: Iron deficiency is an enduring global health problem that requires new remedial approaches. Iron absorption from soybean-derived ferritin, an ∼550-kDa iron storage protein, is comparable to bioavailable ferrous sulfate (FeSO4). However, the absorption of ferritin is reported to involve an endocytic mechanism, independent of divalent metal ion transporter 1 (DMT-1), the transporter for nonheme iron. Objective: Our overall aim was to examine the potential of purified ferritin from peas (Pisum sativum) as a food supplement by measuring its stability under gastric pH treatment and the mechanisms of iron uptake into Caco-2 cells. Methods: Caco-2 cells were treated with native or gastric pH-treated pea ferritin in combination with dietary modulators of nonheme iron uptake, small interfering RNA targeting DMT-1, or chemical inhibitors of endocytosis. Cellular ferritin formation, a surrogate measure of iron uptake, and internalization of pea ferritin with the use of specific antibodies were measured. The production of reactive oxygen species (ROS) in response to equimolar concentrations of native pea ferritin and FeSO4 was also compared. Results: Pea ferritin exposed to gastric pH treatment was degraded, and the released iron was transported into Caco-2 cells by DMT-1. Inhibitors of DMT-1 and nonheme iron absorption reduced iron uptake by 26-40%. Conversely, in the absence of gastric pH treatment, the iron uptake of native pea ferritin was unaffected by inhibitors of nonheme iron absorption, and the protein was observed to be internalized in Caco-2 cells. Chlorpromazine (clathrin-mediated endocytosis inhibitor) reduced the native pea ferritin content within cells by ∼30%, which confirmed that the native pea ferritin was transported into cells via a clathrin-mediated endocytic pathway. In addition, 60% less ROS production resulted from native pea ferritin in comparison to FeSO4. Conclusion: With consideration that nonheme dietary inhibitors display no effect on iron uptake and the low oxidative potential relative to FeSO4, intact pea ferritin appears to be a promising iron supplement.


Subject(s)
Endocytosis , Ferritins/pharmacokinetics , Gastric Acid , Iron/metabolism , Pisum sativum/chemistry , Plant Proteins/pharmacokinetics , Stomach/chemistry , Anemia, Iron-Deficiency/drug therapy , Biological Availability , Biological Transport , Caco-2 Cells , Cation Transport Proteins/metabolism , Diet , Dietary Proteins/isolation & purification , Dietary Proteins/metabolism , Dietary Proteins/pharmacokinetics , Dietary Proteins/therapeutic use , Dietary Supplements , Ferritins/isolation & purification , Ferritins/metabolism , Ferritins/therapeutic use , Humans , Hydrogen-Ion Concentration , Intestinal Absorption , Plant Proteins/isolation & purification , Plant Proteins/metabolism , Plant Proteins/therapeutic use , Reactive Oxygen Species/metabolism , Glycine max/chemistry
9.
Molecules ; 23(2)2018 Feb 12.
Article in English | MEDLINE | ID: mdl-29439533

ABSTRACT

Some molecular and functional properties of albumin (83.6% protein), globulin (95.5% protein), glutelin (81.3% protein) as well as protein isolate (80.7% protein) from cashew nut were investigated. These proteins were subjected to molecular (circular dichroism, gel electrophoresis, scanning electron microscopy) and functional (solubility, emulsification, foaming, water/oil holding capacity) tests. Cashew nut proteins represent an abundant nutrient with well-balanced amino acid composition and could meet the requirements recommended by FAO/WHO. SDS-PAGE pattern indicated cashew nut proteins were mainly composed of a polypeptide with molecular weight (MW) of 53 kDa, which presented two bands with MW of 32 and 21 kDa under reducing conditions. The far-UV CD spectra indicated that cashew proteins were rich in ß-sheets. The surface hydrophobicity of the protein isolate was higher than that of the protein fractions. In pH 7.0, the solubility of protein fractions was above 70%, which was higher than protein isolate at any pH. Glutelin had the highest water/oil holding capacity and foaming properties. Protein isolate displayed better emulsifying properties than protein fractions. In summary, cashew nut kernel proteins have potential as valuable nutrition sources and could be used effectively in the food industry.


Subject(s)
Albumins/chemistry , Anacardium/chemistry , Dietary Proteins/chemistry , Globulins/chemistry , Glutens/chemistry , Nuts/chemistry , Plant Proteins/chemistry , Albumins/isolation & purification , Dietary Proteins/isolation & purification , Electrophoresis, Polyacrylamide Gel , Food Analysis , Globulins/isolation & purification , Glutens/isolation & purification , Hydrogen-Ion Concentration , Molecular Weight , Plant Proteins/isolation & purification , Protein Conformation, beta-Strand , Solubility
10.
Anal Chim Acta ; 1000: 214-222, 2018 Feb 13.
Article in English | MEDLINE | ID: mdl-29289313

ABSTRACT

Arrays of microwells are widely used to isolate individual cells, facilitate high throughput cytometry assays, and ensure compatibility of those assays with whole-cell imaging. Microwell geometries have recently been utilized for handling and preparation of single-cell lysate, prior to single-cell protein electrophoresis. It is in the context of single-cell electrophoresis that we investigate the interplay of microwell geometry (circular, rectangular, triangular) and transport (diffusion, electromigration) on the subsequent performance of single-cell polyacrylamide gel electrophoresis (PAGE) for protein targets. We define and measure injector-induced dispersion during PAGE, and develop a numerical model of band broadening sources, experimentally validate the numerical model, and then identify operating conditions (characterized through the Peclet number, Pe) that lead to microwell-geometry induced losses in separation performance. With analysis of mammalian cells as a case study, we sought to understand at what Pe is the PAGE separation performance adversely sensitized to the microwell geometry. In developing design rules, we find that for the microwell geometries that are the most suitable for isolation of mammalian cells and moderate mass protein targets, the Pe is usually small enough (Pe < âˆ¼20) to mitigate the effect of the microwell geometry on protein PAGE of single-cell lysate. In extreme cases where the largest mammalian cells are analyzed (Pe > âˆ¼20), consideration of Pe suggests using a rectangular - and not the widely used circular - microwell geometry to maximize protein PAGE separation performance.


Subject(s)
Dietary Proteins/isolation & purification , Flow Injection Analysis , Single-Cell Analysis , Animals , Dietary Proteins/chemistry , Electrophoresis, Polyacrylamide Gel , Female , Flow Injection Analysis/instrumentation , Humans , Male , Optical Imaging , Single-Cell Analysis/instrumentation
11.
Food Res Int ; 99(Pt 3): 1028-1035, 2017 09.
Article in English | MEDLINE | ID: mdl-28865613

ABSTRACT

Spirulina platensis is considered an alternative and excellent source of protein [46-63% dry basis (DB)], having protein levels comparable to meat and soybeans. Thus, it can be considered an adequate ingredient to supply the necessity of this compound in the food industry. Its carbohydrates (8-14% DB) may also be a useful food ingredient or a potential source of bioenergy. Thus, extracting these compounds from the microalgae biomass will maximize its exploitation. Sonication can completely or partially degrade the microalgal cell wall, providing a useful technique to extract the protein and carbohydrate. This study used a sequential strategy of experimental design (fractional factorial design and central composite rotatable design) to evaluate the protein and carbohydrate extraction from S. platensis defatted biomass using ultrasonic waves and mechanical agitation, under alkaline conditions. The optimal conditions for protein and carbohydrate co-extraction were established by selecting and maximizing the variables that significantly influenced the extraction. The optimized percentages recovery from the extraction process yielded 75.76% protein and 41.52% carbohydrate at 33-40min sonication and 40-55min agitation. The protein fraction may be further concentrated and purified for use in food formulations, and the carbohydrates may be a useful feedstock for bioethanol production.


Subject(s)
Bacterial Proteins/isolation & purification , Dietary Carbohydrates/isolation & purification , Dietary Proteins/isolation & purification , Dietary Supplements , Food Additives/isolation & purification , Food Handling/methods , Industrial Microbiology/methods , Microalgae/metabolism , Sonication , Spirulina/metabolism , Ultrasonics/methods , Biomass , Microalgae/growth & development , Spirulina/growth & development
12.
J Sci Food Agric ; 97(3): 724-732, 2017 Feb.
Article in English | MEDLINE | ID: mdl-27507218

ABSTRACT

The high protein level of various microalgal species is one of the main reasons to consider them an unconventional source of this compound. Spirulina platensis stands out for being one of the richest protein sources of microbial origin (460-630 g kg-1 , dry matter basis), having similar protein levels when compared to meat and soybeans. The use of S. platensis in food can bring benefits to human health owing to its chemical composition, since it has high levels of vitamins, minerals, phenolics, essential fatty acids, amino acids and pigments. Furthermore, the development of new protein sources to supply the shortage of this nutrient is an urgent need, and protein from S. platensis plays an important role in this scenario. In this sense, extraction processes that allow maximum protein yield and total utilization of biomass is an urgent need, and ultrasonic waves have proven to be an effective extraction technique. The number of scientific papers related to protein fraction from S. platensis is still limited; thus further studies on its functional and technological properties are needed. © 2016 Society of Chemical Industry.


Subject(s)
Bacterial Proteins/therapeutic use , Dietary Proteins/therapeutic use , Food Supply , Global Health , Microalgae/chemistry , Spirulina/chemistry , Amino Acids/analysis , Animal Feed/adverse effects , Animal Feed/economics , Animals , Bacterial Proteins/biosynthesis , Bacterial Proteins/chemistry , Bacterial Proteins/isolation & purification , Dietary Proteins/chemistry , Dietary Proteins/economics , Dietary Proteins/isolation & purification , Evidence-Based Practice , Fermentation , Food Contamination/prevention & control , Food Supply/economics , Food Supply/history , History, 20th Century , History, 21st Century , Humans , Microalgae/growth & development , Microalgae/isolation & purification , Microalgae/metabolism , Nutritive Value , Photobioreactors , Protein Deficiency/economics , Protein Deficiency/prevention & control , Spirulina/growth & development , Spirulina/isolation & purification , Spirulina/metabolism
13.
Aliment Pharmacol Ther ; 45(3): 427-433, 2017 02.
Article in English | MEDLINE | ID: mdl-27878833

ABSTRACT

BACKGROUND: Although eosinophilic oesophagitis (EoE) is putatively mediated by an abnormal response to food antigen, the oesophagus is considered relatively impermeable to large molecules. AIM: To assess whether food antigens penetrate the oesophageal mucosa in patients with EoE. METHODS: Anti-gliadin staining was performed in three groups: active EoE, inactive EoE and EoE patients on a low or gluten free diet. To appraise the specificity of our results, we also performed gliadin staining on six patients without oesophageal disease who were consuming gluten. The groups with EoE on gluten also underwent endoscopic infusion with gluten containing soy sauce and repeat biopsies during the endoscopy. We measured eosinophil density, dilated intercellular spaces (on a 0-4+ scale) and gliadin in oesophageal mucosa by immunofluorescence. RESULTS: Patients with active EoE had significantly greater epithelial density of anti-gliadin staining when compared to inactive EoE (P < 0.0065) and gluten-free patients (P < 0.0008) at baseline and after soy infusion. Gliadin was not detected in non-EoE control patients. The distribution of gliadin was both cytoplasmic and nuclear. There was good correlation of dilated intercellular spaces grade and total gliadin staining intensity (r = 0.577, P = 0.0077). Acute oesophageal perfusion of a commercial gliadin-rich soy sauce did not lead to an increase in gliadin staining in active or inactive EoE. CONCLUSION: These findings suggest, although do not prove, that antigen penetration in active eosinophilic oesophagitis might be facilitated by impairment of epithelial integrity.


Subject(s)
Antigens/isolation & purification , Dietary Proteins/isolation & purification , Eosinophilic Esophagitis/pathology , Mouth Mucosa/chemistry , Adolescent , Adult , Antigens/metabolism , Biopsy , Dietary Proteins/immunology , Dietary Proteins/metabolism , Disease Progression , Eosinophilic Esophagitis/complications , Eosinophilic Esophagitis/immunology , Eosinophilic Esophagitis/metabolism , Eosinophils/pathology , Extracellular Space/immunology , Extracellular Space/metabolism , Female , Food Hypersensitivity/complications , Food Hypersensitivity/immunology , Food Hypersensitivity/metabolism , Food Hypersensitivity/pathology , Humans , Male , Middle Aged , Mouth Mucosa/immunology , Mouth Mucosa/metabolism , Mouth Mucosa/pathology , Sensitivity and Specificity , Young Adult
14.
J Sci Food Agric ; 97(3): 811-817, 2017 Feb.
Article in English | MEDLINE | ID: mdl-27185206

ABSTRACT

BACKGROUND: Protein may be recovered by using pH shifts to solubilize and precipitate protein. Typically, sodium hydroxide is used as the processing base; however, this has been shown to significantly increase sodium in the final recovered protein. RESULTS: Protein was extracted from black bullhead catfish (Ameiurus melas) using a pH-shift method. Protein was solubilized using either sodium hydroxide (NaOH) or calcium hydroxide (Ca(OH)2 ) and precipitated at pH 5.5 using hydrochloric acid (HCl). Protein solubility was greater when Ca(OH)2 was used compared to NaOH during this process. Using Ca(OH)2 as the processing base yielded the greatest lipid recovery (P < 0.05) at 77 g 100 g-1 , whereas the greatest (P < 0.05) protein recovery yield was recorded as 53 g 100 g-1 protein using NaOH. Protein solubilized with Ca(OH)2 had more (P < 0.05) calcium in the protein fraction, whereas using NaOH increased (P < 0.05) sodium content. CONCLUSION: Results of our study showed that protein solubility was increased and the recovered protein had significantly more calcium when Ca(OH)2 was used as the processing base. Results showed both NaOH and Ca(OH)2 to be an effective processing base for pH-shift protein recovery processes. © 2016 Society of Chemical Industry.


Subject(s)
Calcium Hydroxide/chemistry , Dietary Proteins/isolation & purification , Fish Products/analysis , Fish Proteins/isolation & purification , Food Additives/chemistry , Ictaluridae , Animals , Calcium, Dietary/analysis , Chemical Precipitation , Dietary Fats/analysis , Dietary Proteins/chemistry , Fish Proteins/chemistry , Fisheries , Food Handling , Food Packaging , Food Storage , Humans , Hydrochloric Acid/chemistry , Hydrogen-Ion Concentration , Nutritive Value , Sodium Hydroxide/chemistry , Solubility , Vacuum , West Virginia
15.
Carbohydr Polym ; 152: 231-240, 2016 Nov 05.
Article in English | MEDLINE | ID: mdl-27516269

ABSTRACT

The objective of this work was to fit together the starch extraction from Pachyrhizus ahipa roots and the recovery of the proteins present in these storage organs, making an improved use of this novel raw material. The replacement of water by buffer PO4(-3)/NaCl as solvent in the first extraction steps improved protein extraction without lowering the starch yield. The starches obtained from the traditional and the proposed methods exhibited some differences in appearance and technological and thermal properties, which were endorsed to the adjustment in the methodology of extraction rather than to the use of buffer as solvent. Thus, P. ahipa starch obtaining procedure could be coupled to protein extraction with a minimum change in the methodology. This innovation did not significantly shift the characteristics of the starch obtained and allowed to obtain a protein yield of 135.7mg BSA equivalent protein/100g of fresh roots.


Subject(s)
Pachyrhizus/chemistry , Plant Proteins/isolation & purification , Plant Roots/chemistry , Starch/isolation & purification , Dietary Proteins/isolation & purification , Fabaceae/chemistry , Solvents , Vegetables/chemistry , Water/chemistry
16.
J Oleo Sci ; 65(4): 319-29, 2016.
Article in English | MEDLINE | ID: mdl-26972462

ABSTRACT

In this study, proteins of the defatted meals obtained from cold-pressed poppyseed previously treated (pre-roasting and enzyme against control) were extracted and their compositional and functional properties were determined. Saline-alkaline extraction (pH 11-12, and 0.2-0.6 M NaCI) and isoelectric point (pH 4.0-5.5) precipitation technique showed that seed pre-roasting enhances protein yield while enzyme treatment reduces it. There were 7 bands on SDS-PAGE, and enzyme treated samples were weaker than control. While enzyme treatment decreased denaturation temperatures (T(d)), roasting enhanced the enthalpy change (ΔH) values. Pre-treatments caused a decrease in protein least gelling concentration (LGC) values. Water and oil holding capacities (WHC and OHC) were found lower in enzyme treated and higher in preroasted samples. Similar effects were also determined for emulsifying activity (EA) and emulsion stability (ES) values. While foaming capacity (FC) in treated samples decreased, foam stability (FS) increased oppositely. In conclusion, poppyseed meals can be nutritionally good source for diet protein, and a limited pre-roasting can be very beneficial for enhanced protein extraction yield and desirable functional properties.


Subject(s)
Dietary Proteins/isolation & purification , Food Handling , Glycoside Hydrolases , Papaver/chemistry , Peptide Hydrolases , Plant Proteins/isolation & purification , Dietary Proteins/chemistry , Emulsions , Isoelectric Point , Plant Oils/analysis , Plant Proteins/chemistry , Temperature , Water/analysis
17.
Meat Sci ; 111: 60-6, 2016 Jan.
Article in English | MEDLINE | ID: mdl-26340742

ABSTRACT

Oxidation is a major cause of protein quality deterioration during the storage and processing of food. This study investigated the effects of clove extract (CE) on structural and rheological changes in porcine longissimus myofibrillar proteins (MP) and the effects of oxidizing radicals produced by a Fenton reaction system (FRS). Increased oxidation time was accompanied by increased carbonyl content, reduced Ca-ATPase activity, decreased enthalpy of denaturation, decreased thermal transition temperatures (P<0.05), and increased protein susceptibility to thermal aggregation. The addition of CE significantly inhibited carbonyl formation (P<0.05), enhanced solubility and thermal stability, and improved the gel formation ability (storage modulus, loss modulus) of MP. The protective effect of CE on protein denaturation was demonstrated by its efficacy in maintaining Ca-ATPase activity and decreasing the degree of protein aggregation. Overall, the hydroxyl radical-induced loss of the structural and functional properties of MP was significantly reduced by the presence of CE.


Subject(s)
Antioxidants/chemistry , Dietary Proteins/chemistry , Food Preservatives/chemistry , Meat/analysis , Muscle Proteins/chemistry , Plant Extracts/chemistry , Syzygium/chemistry , Animals , Antioxidants/isolation & purification , Calorimetry, Differential Scanning , China , Dietary Proteins/analysis , Dietary Proteins/isolation & purification , Flowers/chemistry , Flowers/growth & development , Food Preservatives/isolation & purification , Gels , Hydroxyl Radical/analysis , Hydroxyl Radical/antagonists & inhibitors , Hydroxyl Radical/chemistry , Meat/economics , Muscle Proteins/analysis , Muscle Proteins/isolation & purification , Oxidation-Reduction , Plant Extracts/isolation & purification , Protein Carbonylation , Protein Conformation , Protein Stability , Rheology , Solubility , Sus scrofa , Syzygium/growth & development , Transition Temperature , Viscosity
18.
Crit Rev Food Sci Nutr ; 56(1): 92-112, 2016.
Article in English | MEDLINE | ID: mdl-25569557

ABSTRACT

Bioactive peptides are food derived components, usually consisting of 3-20 amino acids, which are inactive when incorporated within their parent protein. Once liberated by enzymatic or chemical hydrolysis, during food processing and gastrointestinal transit, they can potentially provide an array of health benefits to the human body. Owing to an unprecedented increase in the worldwide incidence of obesity and hypertension, medical researchers are focusing on the hypotensive and anti-obesity properties of nutritionally derived bioactive peptides. The role of the renin-angiotensin system has long been established in the aetiology of metabolic diseases and hypertension. Targeting the renin-angiotensin system by inhibiting the activity of angiotensin-converting enzyme (ACE) and preventing the formation of angiotensin II can be a potential therapeutic approach to the treatment of hypertension and obesity. Fish-derived proteins and peptides can potentially be excellent sources of bioactive components, mainly as a source of ACE inhibitors. However, increased use of marine sources, poses an unsustainable burden on particular fish stocks, so, the underutilized fish species and by-products can be exploited for this purpose. This paper provides an overview of the techniques involved in the production, isolation, purification, and characterization of bioactive peptides from marine sources, as well as the evaluation of the ACE inhibitory (ACE-I) activity and bioavailability.


Subject(s)
Anti-Obesity Agents/therapeutic use , Antihypertensive Agents/therapeutic use , Aquatic Organisms/chemistry , Drug Discovery , Peptide Fragments/therapeutic use , Animals , Anti-Obesity Agents/economics , Anti-Obesity Agents/isolation & purification , Anti-Obesity Agents/metabolism , Antihypertensive Agents/economics , Antihypertensive Agents/isolation & purification , Antihypertensive Agents/metabolism , Dietary Proteins/chemistry , Dietary Proteins/isolation & purification , Dietary Proteins/metabolism , Dietary Proteins/therapeutic use , Dietary Supplements/economics , Drug Discovery/trends , Fish Proteins/chemistry , Fish Proteins/isolation & purification , Fish Proteins/metabolism , Fish Proteins/therapeutic use , Food-Processing Industry/economics , Humans , Hypertension/diet therapy , Hypertension/drug therapy , Industrial Waste/analysis , Industrial Waste/economics , Obesity/diet therapy , Obesity/drug therapy , Oligopeptides/economics , Oligopeptides/isolation & purification , Oligopeptides/metabolism , Oligopeptides/therapeutic use , Peptide Fragments/economics , Peptide Fragments/isolation & purification , Peptide Fragments/metabolism , Proteolysis
19.
Crit Rev Food Sci Nutr ; 56(5): 760-87, 2016.
Article in English | MEDLINE | ID: mdl-25036695

ABSTRACT

Year to year obesity prevalence, reduced physical activities, bad habits/or stressful lifestyle, and other environmental and physiological impacts lead to increase in diseases such as coronary heart disease, stroke, cancer, diabetes, and hypertension worldwide. Hypertension is considered as one of the most common serious chronic diseases; however, discovery of medications with high efficacy and without side effects for treatment of patients remains a challenge for scientists. Recent trends in functional foods have evidenced that food bioactive proteins play a major role in the concepts of illness and curing; therefore, nutritionists, biomedical scientists, and food scientists are working together to develop improved systems for the discovery of peptides with increased potency and therapeutic benefits. This review presents a recent research carried out to date for the purpose of isolation and identification of bioactive hydrolyzates and peptides with angiotensin I converting enzyme inhibitory activity and antihypertensive effect from animal, marine, microbial, and plant food proteins. Effects of food processing and hydrolyzation conditions as well as some other impacts on formation, activity, and stability of these hydrolyzates and peptides are also presented.


Subject(s)
Antihypertensive Agents/pharmacology , Dietary Proteins/pharmacology , Protein Hydrolysates/pharmacology , Angiotensin-Converting Enzyme Inhibitors/isolation & purification , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Blood Pressure/drug effects , Dietary Proteins/isolation & purification , Disease Models, Animal , Egg Proteins/isolation & purification , Egg Proteins/pharmacology , Fishes , Food Analysis , Food Handling , Fruit/chemistry , Humans , Hypertension/drug therapy , Meat/analysis , Milk/chemistry , Milk Proteins/isolation & purification , Milk Proteins/pharmacology , Plant Proteins/isolation & purification , Plant Proteins/pharmacology , Protein Hydrolysates/isolation & purification , Seafood/analysis , Vegetables/chemistry
20.
Curr Protein Pept Sci ; 16(7): 613-21, 2015.
Article in English | MEDLINE | ID: mdl-26122781

ABSTRACT

Soybean is widely utilized in the food and feed industries. However, soybean contains many anti-nutritional factors that limit its extended application. The two most important antigenic proteins are glycinin and ß-conglycinin. When young animals are fed diets containing soybean protein, a small portion of undigested proteins enters the lymph and blood through gaps between the intestinal epithelial cells. These macromolecules have considerable antigenic activity and stimulate the immune system resulting in specific antigen-antibody reactions and T lymphoid cell-mediated delayed hypersensitivity. A current focus of research is to develop methods to decrease the immuno-reactivity of soybean proteins. Several strategies have been developed to prevent food allergies including those feed processing and plant breeding. The latest studies indicate that certain kinds of immuno-modulators, such as vitamin C and lipoic acid, may specifically block the IgE mediated anaphylaxis and these may provide new insight into the effective prevention of soybean-induced allergy and perhaps other food allergies. This review is divided into seven parts including (1) Allergenic proteins found in soybean; (2) Structure-function relationships of allergenic proteins in soybean; (3) Extraction, purification and detection of allergenic proteins in soybean; (4) Anaphylaxis induced by allergenic proteins in soybean; (5) The potential mechanism of soybean allergy; (6) Prevention and treatment of soybean allergy; (7) The effects of plant breeding on the antigenicity of allergen proteins in soybean. Being fully aware of the soy protein antigen and finding the methods to eliminate anaphylaxis induced by soybean proteins will help to significantly improve efficiency of soybean protein utilization.


Subject(s)
Antigens, Plant/immunology , Glycine max/immunology , Intestines/immunology , Anaphylaxis/immunology , Anaphylaxis/prevention & control , Animals , Antigens, Plant/isolation & purification , Dietary Proteins/immunology , Dietary Proteins/isolation & purification , Food Hypersensitivity/immunology , Humans , Plant Proteins/immunology , Plant Proteins/isolation & purification
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