Chickpea Protein Isolation, Characterization and Application in Muffin Enrichment

The aim of this study was to enhance the nutritional value and the functional characteristics of muffins by enriching with chickpea protein isolate, while keeping their rheological characteristics. Chickpea Protein isolate (CPI) was prepared by alkaline solubilization (pH 11), followed by isoelectric precipitation at pH 4.5. SDS-PAGE revealed three subunits with molecular weights of 47, 30 and 85 kDa; representing the globulin fractions, legumin-like and vicilin-like proteins. Maximum protein solubility (83.32%) was obtained at pH 11. CPI exhibited an emulsifying activity index of 25.17 m2 g-1, emulsion stability index of 14.09 min. The foaming capacity and stability were 62% and 94.49%, respectively. Water and oil absorption were 3.65 and 2.30 mL g-1, respectively. CPI was added to muffin batter at 0, 2.5, 5, 7.5 and 10%. CPI fortifieded muffins showed reduction in moisture content, which influenced texture profile analysis through increasing hardness, gumminess and chewiness values. Additionally, both protein content and protein digestibility of muffins increased to 22.2 and 94.08%, respectively. CPI-enriched muffins were darker (lower L) with yellowish crumbs (higher b). Finally, preliminary sensory evaluation showed high consumer acceptance for CPI-enriched muffins.

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Combined Effects of Calcium Addition and Thermal Processing on the Texture and In Vitro Digestibility of Starch and Protein of Black Beans (Phaseolus vulgaris)

Foods ◽

10.3390/foods10061368 ◽

2021 ◽

Vol 10 (6) ◽

pp. 1368

Author(s):

Marbie Alpos ◽

Sze Ying Leong ◽

Indrawati Oey

Keyword(s):

Thermal Processing ◽

Profile Analysis ◽

Protein Digestibility ◽

In Vitro Digestibility ◽

Texture Profile ◽

Black Beans ◽

Calcium Addition ◽

The Impact ◽

Cacl2 Solution

Legumes are typically soaked overnight to reduce antinutrients and then cooked prior to consumption. However, thermal processing can cause over-softening of legumes. This study aimed to determine the effect of calcium addition (0, 100, 300, and 500 ppm in the form of calcium chloride, CaCl2), starting from the overnight soaking step, in reducing the loss of firmness of black beans during thermal processing for up to 2 h. The impact of calcium addition on the in vitro starch and protein digestibility of cooked beans was also assessed. Two strategies of calcium addition were employed in this study: (Strategy 1/S1) beans were soaked and then cooked in the same CaCl2 solution, or (Strategy 2/S2) cooked in a freshly prepared CaCl2 solution after the calcium-containing soaking medium was discarded. Despite the texture degradation of black beans brought about by increasing the cooking time, texture profile analysis (TPA) revealed that their hardness, cohesiveness, springiness, chewiness, and resilience improved significantly (p < 0.05) with increasing calcium concentration. Interestingly, beans cooked for 2 h with 300 ppm CaCl2 shared similar hardness with beans cooked for 1 h without calcium addition. Starch and protein digestibility of calcium-treated beans generally improved with prolonged cooking. However, calcium-treated beans cooked for 1 h under S2 achieved a reduced texture loss and a lower starch digestibility than those beans treated in S1. A lower starch digestion could be desired as this reflects a slow rise in blood glucose levels. Findings from this result also showed that treating black beans with high level of CaCl2 (i.e., 500 ppm) was not necessary, otherwise this would limit protein digestibility of cooked black beans.

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Fabricating a Pickering Stabilizer from Okara Dietary Fibre Particulates by Conjugating with Soy Protein Isolate via Maillard Reaction

Foods ◽

10.3390/foods9020143 ◽

2020 ◽

Vol 9 (2) ◽

pp. 143 ◽

Cited By ~ 3

Author(s):

Tolulope Joshua Ashaolu ◽

Guohua Zhao

Keyword(s):

Maillard Reaction ◽

Soy Protein ◽

Dietary Fibre ◽

Activity Index ◽

Soy Protein Isolate ◽

Stability Index ◽

Amino Acid Profile ◽

Protein Isolate ◽

Interfacial Behaviour ◽

Droplet Sizes

Okara is underutilized despite its numerous values explorable in food products. In this study, okara dietary fibre (ODF) was micronized and decorated with soy protein isolate (SPI) through a Maillard reaction by dry heating at 60 °C. The resulting ODF-SPI conjugates were thermally stable, hydrophilic rather than hydrophobic, and exhibited excellent Pickering emulsion stabilization potentials as indicated in their interfacial behaviour, microstructure, droplet sizes, emulsifying activity index (EAI) and emulsion stability index (ESI). In addition, the conjugates’ structure–function relationships, amino acid profile, and emulsifying potentials are indicative of being employed in the formulation of emulsion-based foods or non-edible products.

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Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation

Foods ◽

10.3390/foods9060703 ◽

2020 ◽

Vol 9 (6) ◽

pp. 703

Author(s):

Hristo Kalaydzhiev ◽

Radoslav Georgiev ◽

Petya Ivanova ◽

Magdalena Stoyanova ◽

Cristina L. M. Silva ◽

...

Keyword(s):

Protein Solubility ◽

Rapeseed Meal ◽

Protein Isolate ◽

Protein Fractions ◽

Isoelectric Precipitation ◽

Protein Isolates ◽

Sds Page ◽

Enhanced Solubility ◽

Meal Protein ◽

Biochemical Analyses

The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates.

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INFLUENCE OF DREGEA SINENSIS HEMSL. PROTEASE ON THE QUALITY OF MOZZARELLA CHEESE FROM BUFFALO MILK

Emirates Journal of Food and Agriculture ◽

10.9755/ejfa.2016-09-1227 ◽

2017 ◽

pp. 539 ◽

Cited By ~ 3

Author(s):

Hongyan Wang ◽

Yujing Wang ◽

Aixiang Huang

Keyword(s):

Profile Analysis ◽

Buffalo Milk ◽

Control Group ◽

Mozzarella Cheese ◽

Texture Profile ◽

Sds Page ◽

Small Pore ◽

Process Cheese ◽

Enzyme Source

Dregea sinensis Hemsl. protease, a new enzyme source, is described with the characteristics of milk curd. However, cheese processing with this protease has yet to be described. In this study, a protease called chymosin was extracted and purified from D. sinensis Hemsl. stalk. Calf rennet and microbial chymosin were used as the control group in the production of mozzarella cheese to investigate the effect of this plant species on the quality of cheese. Results: SDS-PAGE revealed that D. sinensis Hemsl. protease can be used to process cheese because this enzyme elicits a degradation effect on α-casein in mozzarella cheese. Fresh and sweet glutamic acid and histidine are the dominant free amino acids in mozzarella cheese (P<0.5). Fifty-two flavor substances were detected through GC-MS. Volatile acids and carbonyl compounds are the main sources of the flavor of mozzarella cheese. Texture profile analysis indicated that the produced cheese was more restorative and flexible. Scanning electron microscopy demonstrated that the produced cheese was smooth, as indicated by the small pore cross-section diameter of mozzarella cheese and its close net structure. Therefore, D. sinensis Hemsl. can be applied to process cheese.

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Effects of Cavitation Jet Treatment on the Structure and Emulsification Properties of Oxidized Soy Protein Isolate

Foods ◽

10.3390/foods10010002 ◽

2020 ◽

Vol 10 (1) ◽

pp. 2

Author(s):

Mingyu He ◽

Changling Wu ◽

Lijia Li ◽

Li Zheng ◽

Tian Tian ◽

...

Keyword(s):

Particle Size ◽

Soy Protein ◽

Activity Index ◽

Soy Protein Isolate ◽

Sulfhydryl Group ◽

Stability Index ◽

Surface Hydrophobicity ◽

Protein Isolate ◽

Atomic Force ◽

Α Helix

This study examined the ability of cavitation jet processing to regulate the oxidation concentrations with 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH) (0.2, 1, and 5 mmol/L) and the structure and emulsification of soy protein isolate (SPI). The tested properties included particle size distribution, hydrophobic properties (sulfhydryl group (SH) and disulfide bond (S-S) contents, surface hydrophobicity (H0)), emulsifying properties (particle size and ζ-potential of emulsions, emulsification activity index (EAI), and emulsification stability index (ESI)), as well as conformational characteristics. The high shear force of cavitation jet treatment reduced the particle size of oxidized SPI and distributed uniformly. Cavitation jet (90 MPa)-treated SPI (AAPH with 1 mmol/L) demonstrated a high H0 (4688.70 ± 84.60), high EAI (71.78 ± 1.52 m2/g), and high ESI (86.73 ± 0.97%). The ordered secondary structure (α-helix and β-turn content) of SPI was enhanced by the cavitation jet. Meanwhile, the distribution of SPI-oxidized aggregates was observed under an atomic force microscope. Therefore, cavitation jet processing combined with oxidation treatment is an effective method to improve the characteristics of SPI and has potential industrial application prospects.

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Effects of Extruded Soy Protein on the Quality of Chinese Steamed Bread

Journal of Chemistry ◽

10.1155/2016/3691523 ◽

2016 ◽

Vol 2016 ◽

pp. 1-8 ◽

Cited By ~ 7

Author(s):

Zhenya Du ◽

Fusheng Chen ◽

Kunlun Liu ◽

Shaojuan Lai ◽

Lifen Zhang ◽

...

Keyword(s):

Soy Protein ◽

Profile Analysis ◽

Positive Trend ◽

Chinese Steamed Bread ◽

Texture Profile ◽

Soy Protein Isolates ◽

Sds Page ◽

Sensory Score ◽

Steamed Bread

Five different extruded soy protein isolates (ESPIs) were obtained by extrusion and denoted by IVD1, IVD2, IVD3, IVD4, and IVD5. Then the SDS-PAGE results showed that the subunits of SPI decreased after extrusion, especially the subunits of 90.8, 32.8, and 31.3 kDa, whereas no isopeptide bond was formed. Although SPI improved both the development time (DT) and stability (S) of dough, ESPIs increasedSbut the DT decreased from 4.3 min to 1.8–2.0 min. Texture profile analysis (TPA) results showed that the hardness and chewiness of Chinese steamed bread (CSB) decreased in the order wheat flour+IVD2 (WF+IVD2), WF+SPI, WF+IVD4, WF+IVD1, WF+IVD3, WF, and WF+IVD5. As regards color, the total colorΔEdecreased except for the WF+IVD1 (56.22); its positive and negative trends ofL⁎andb⁎were invariant with the SPI or ESPIs mixture, whereasa⁎showed a positive trend. The sensory score increased from 82.7 to 83.4 with 3% of SPI addition and up to 87.8 when the substitution was IVD1. Therefore, SPI treated by extrusion may significantly improve the quality of CSB.

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Structural and Functional Changes in Ultrasonicated Oyster Protein Isolates

International Journal of Food Engineering ◽

10.1515/ijfe-2018-0190 ◽

2019 ◽

Vol 15 (3-4) ◽

Cited By ~ 1

Author(s):

Cuiping Yu ◽

Fan Wu ◽

Yue Cha ◽

Henan Zou ◽

Yingnan Guo ◽

...

Keyword(s):

Particle Size ◽

Functional Properties ◽

Activity Index ◽

Protein Solubility ◽

Stability Index ◽

Protein Isolates ◽

Complex Needs ◽

Functional Changes ◽

Structural And Functional Properties ◽

Water Holding

AbstractStructural and functional changes in ultrasonicated oyster protein isolates (OPI) were investigated. Ultrasound treatments were carried out with probe (20 kHz) at 200, 400 and 600 W for 15 and 30 min. The results showed that functional properties of OPI significantly improved after sonication. Absolute zeta potential and protein solubility increased by 18.40 mV and 82.5 % at 600 W for 15 min. Oil holding capacity, emulsifying activity index, emulsion stability index, foaming ability and foaming stability increased by 300 %, 15.23 m2/g, 9.24 min, 23.9 % and 14.8 % at 600 W for 30 min. However, ultrasound treatment significantly (P < 0.05) decreased particle size and water holding capacity. The conformation of OPI became stretched and unfolded after sonication. Functional improvements resulted from stretched and unfolded conformation and reduction of particle size. Controlled condition of ultrasound can produce OPI with distinct structural and functional properties, which could meet the complex needs of manufactured food products in food industry, but further study is needed to understand the specific mechanism.

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Comparison of Thermal and High-Pressure Gelation of Potato Protein Isolates

Foods ◽

10.3390/foods9081041 ◽

2020 ◽

Vol 9 (8) ◽

pp. 1041

Author(s):

Hadas Katzav ◽

Libi Chirug ◽

Zoya Okun ◽

Maya Davidovich-Pinhas ◽

Avi Shpigelman

Keyword(s):

High Pressure ◽

Profile Analysis ◽

Textural Properties ◽

Protein Isolate ◽

Limited Information ◽

Potato Protein ◽

Texture Profile ◽

Food Applications ◽

Water Holding ◽

Starch Industry

Potato protein isolate (PPI), a commercial by-product of the starch industry, is a promising novel protein for food applications with limited information regarding its techno-functionality. This research focused on the formation of both thermal and high-pressure gels at acidic and neutral pH levels. Our results reveal that physical gels are formed after 30 min by heat at pH 7 and pH 3, while pressure (300–500 MPa) allows the formation of physical gels only at pH 3, and only when the system crosses 30 °C by adiabatic heating during pressurization. Texture profile analysis (TPA) revealed that gel hardness increased with both gelation temperature and pressure, while water-holding capacity was lower for the pressure-induced gels. The proteins released in the water-holding test suggested only partial involvement of patatin in the gel formation. Vitamin C as a model for a thermally liable compound verified the expected better conservation of such compounds in a pressure-induced gel compared to a thermal one of similar textural properties, presenting a possible advantage for pressure-induced gelation.

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The Identification of Main Proteins Fractions from Pea Protein Isolates

Bulletin of University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca Agriculture ◽

10.15835/buasvmcn-agr:3752 ◽

1970 ◽

Vol 66 (2) ◽

Author(s):

Raul IANCHICI ◽

Rodica SEGAL ◽

Simona CRISAN ◽

Monica ZDREMTAN

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Human Body ◽

Nutritional Value ◽

Essential Amino Acids ◽

Protein Isolate ◽

Protein Isolates ◽

Pea Protein ◽

Molecular Weights ◽

Sds Page

Pea’s proteins represent a valuable source of edible proteins which are well tolerating by human body, and contain all essential amino acids. Mature pea’s seeds are very rich in proteins that can be extracted in order to be used to improve the nutritional value of other foods. Pea’s proteins contain several fractions of albumins and globulins. We have used electrophoresis to separate and identify these fractions, to establish the molecular weight of each fraction, and also the proportion between them. The electrophoresis was conducted following the SDS-PAGE protocol. Using pea protein isolate as sample, we have found a number of 12 protein fractions with molecular weights ranging between 12500 and 140000 Daltons. From these, six fractions are prevalent.

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A Novel Approach for Tuning the Physicochemical, Textural, and Sensory Characteristics of Plant-Based Meat Analogs with Different Levels of Methylcellulose Concentration

Foods ◽

10.3390/foods10030560 ◽

2021 ◽

Vol 10 (3) ◽

pp. 560

Author(s):

Allah Bakhsh ◽

Se-Jin Lee ◽

Eun-Yeong Lee ◽

Nahar Sabikun ◽

Young-Hwa Hwang ◽

...

Keyword(s):

Profile Analysis ◽

Control Sample ◽

Texture Profile ◽

Crude Fiber Content ◽

A Value ◽

Novel Approach ◽

Meat Analog ◽

And Control ◽

Water Holding ◽

Different Levels

This study assessed the effects of Methylcellulose (MC) at different concentrations on plant-based meat analog (PBMA) patties, comprised of commercial texture vegetable protein (C-TVP) and textured isolate soy protein (T-ISP) as key ingredients, and compared to beef patty control. A significantly higher difference was observed in moisture content in control with increasing MC concentration than the C-TVP and T-ISP patties. However, protein varied significantly among three different protein sources, with control had higher protein content than PBMA patties. Crude fiber content recorded higher values in C-TVP as compared to control. Significantly lower pH values were recorded in control than C-TVP and T-ISP respectively. Regardless, with the addition of MC or ingredient PBMA and control patties tend to reduce lightness (L*) and redness (a*) value after cooking. Although control sample before cooking exhibits lighter and redder than PBMA patties (C-TVP and T-ISP). Likewise, water holding capacity (WHC) decreases as the concentration of MC increases (1.5–4%) in control and PBMA patties. Warner-Bratzler shear force (WBSF) and texture profile analysis (TPA), including hardness, chewiness, and gumminess of control, were significantly higher than C-TVP and T-ISP. Consequently, panelists’ in the sensory analysis presented that C-TVP patties containing 3% of MC had better sensory properties than T-ISP. Hence, PBMA patties with C-TVP and incorporation of 3% MC are considered ideal for manufacturing of meat analog as related to control (beef).

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