Physicochemical and functional properties of kidney bean albumin and globulin protein fractions

Mundi, Sule; Aluko, Rotimi E.

doi:10.1016/j.foodres.2012.04.006

Cited by 152 publications

(125 citation statements)

References 48 publications

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“…The differences between Arg/Lys values obtained in this work for the Canadian HSPs and the value reported by Tang and others () for the Chinese HPI may be due to variations in genetic and environment factors. Our current values are also higher than the <1 values reported for kidney bean proteins (Mundi and Aluko , ), or the 0.44 value reported for casein and 2.53 to 2.65 values for rice proteins (Yang and others ).…”

Section: Resultscontrasting

confidence: 68%

“…For example, some previous works have studied the physicochemical and functional properties of legume flours, protein isolates, and their 7S globulins in order to determine their potential functionality in foods (Du and others ; MuneMune and others ; Tan and others ). Besides functional properties, plant proteins have also been studied for their physicochemical characteristics such as amino acid composition, hydrophobicity, and polypeptide composition (Mundi and Aluko , ; Tan and others ). Hemp ( Cannabis sativa L.) originated from Central Asia (Girgih and others ) and has been commonly used to produce fibers (Yin and others ) for ropes and fabrics.…”

Section: Introductionmentioning

confidence: 99%

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Structural and Functional Properties of Hemp Seed Protein Products

Malomo

Aluko

2014

Journal of Food Science

203

154

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The effects of pH and protein concentration on some structural and functional properties of hemp seed protein isolate (HPI, 84.15% protein content) and defatted hemp seed protein meal (HPM, 44.32% protein content) were determined. The HPI had minimum protein solubility (PS) at pH 4.0, which increased as pH was decreased or increased. In contrast, the HPM had minimum PS at pH 3.0, which increased at higher pH values. Gel electrophoresis showed that some of the high molecular weight proteins (>45 kDa) present in HPM were not well extracted by the alkali and were absent or present in low ratio in the HPI polypeptide profile. The amino acid composition showed that the isolation process increased the Arg/Lys ratio of HPI (5.52%) when compared to HPM (3.35%). Intrinsic fluorescence and circular dichroism data indicate that the HPI proteins had a well-defined structure at pH 3.0, which was lost as pH value increased. The differences in structural conformation of HPI at different pH values were reflected as better foaming capacity at pH 3.0 when compared to pH 5.0, 7.0, and 9.0. At 10 and 25 mg/mL protein concentrations, emulsions formed by the HPM had smaller oil droplet sizes (higher quality), when compared to the HPI-formed emulsions. In contrast at 50 mg/mL protein concentration, the HPI-formed emulsions had smaller oil droplet sizes (except at pH 3.0). We conclude that the functional properties of hemp seed protein products are dependent on structural conformations as well as protein concentration and pH.

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Section: Resultscontrasting

confidence: 68%

Section: Introductionmentioning

confidence: 99%

Structural and Functional Properties of Hemp Seed Protein Products

Malomo

Aluko

2014

Journal of Food Science

203

154

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“…Tang (2008) reported that 7S-globulin had two different endothermic denaturation temperatures (87.7 and 94.1℃) and that disulfide bonds did not contribute to increase the gelling property; however, hydrophobic and hydrogen bonds mainly affected the gelation. Mundi and Aluko (2012) reported that globulin of kidney bean had higher gel forming ability and emulsion stability than albumin. The exposures of hydrophobic residues induced by heating might increase the protein-protein interactions in globulin of kidney beans and increased the gel forming ability.…”

Section: Resultsmentioning

confidence: 99%

“…Physicochemical, functional, and structural characteristics of these proteins and their 7S globulins were investigated by evaluating the heat stability, protein solubility, pH, surface hydrophobicity, emulsion stability, and secondary structures (Tang and Sun, 2011). Mundi and Aluko (2012) extracted globulins from kidney bean protein fractions and reported higher gelling properties and emulsion stability than albumin. This is partially due to the increased surface hydrophobicity of globulin, which might increase the gelling properties induced by protein-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

Effects of Red Bean (Vigna angularis) Protein Isolates on Rheological Properties of Microbial Transglutaminase Mediated Pork Myofibrillar Protein Gels as Affected by Fractioning and Preheat Treatment

Jang

Chin

2016

Korean Journal for Food Science of Animal Resources

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Fractioning and/or preheating treatment on the rheological properties of myofibrillar protein (MP) gels induced by microbial transglutaminase (MTG) has been reported that they may improve the functional properties. However, the optimum condition was varied depending on the experimental factors. This study was to evaluate the effect of red bean protein isolate (RBPI) on the rheological properties of MP gels mediated by MTG as affected by modifications (fractioning: 7S-globulin of RBPI and/or preheat treatment (pre-heating; 95℃/30 min): pre-heating RBPI or pre-heating/7S-globulin). Cooking yields (CY, %) of MP gels was increased with RBPI (p<0.05), while 7S-globulin decreased the effect of RBPI (p<0.05); however, preheating treatments did not affect the CY (p>0.05). Gel strength of MP was decreased when RBPI or 7S-globulin added, while preheat treatments compensated for the negative effects of those in MP. This effect was entirely reversed by MTG treatment. Although the major band of RBPI disappeared, the preheated 7S globulin band was remained. In scanning electron microscopic (SEM) technique, the appearance of more cross-linked structures were observed when RBPI was prepared with preheating at 95℃ to improve the protein-protein interaction during gel setting of MP mixtures. Thus, the effects of RBPI and 7S-globulin as a substrate, and water and meat binder for MTG-mediated MP gels were confirmed to improve the rheological properties. However, preheat treatment of RBPI should be optimized.

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“…The seed proteins of legumes are mostly albumins and globulins that account for about 40-90% of seed protein, which are water soluble and soluble in dilute neutral salt solutions, respectively [32]. The studied bean varieties may have dissimilar protein profiles; Sánchez-Arteaga et al [33] reported for negro beans a higher proportion of total globulin and glutelins than for flor de mayo and pinto beans.…”

Section: Thickness and Moisturementioning

confidence: 98%

Preparation and Characterization of Proteinaceous Films from Seven Mexican Common Beans (Phaseolus vulgarisL.)

Montalvo-Paquini

Avila‐Sosa

López‐Malo

et al. 2018

Journal of Food Quality

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Bean protein concentrate (BPC) as a protein source from seven varieties of Mexican common beans (alubia, flor de mayo, garbancillo, peruano, pinto, mantequilla, and negro) was utilized for formulating edible films (EF). EF were prepared with BPC (3% w/w) and glycerol as a plasticizer by the casting method; their thickness, water content, soluble matter, protein solubility, color, puncture strength, elongation, water vapor permeability (WVP), and chemical properties (Fourier transform infrared, FTIR, and spectroscopy) were evaluated. Tested EF had an average thickness of 0.045 ± 0.001 mm. Good stability was observed since the studied polymers did not exceed 35% of the total soluble matter while protein solubilities were not greater than 3%. EF made from peruano bean protein presented a lower value of total matter solubility (25.38 ± 2.24%) than the other tested EF. A low value of WVP (2.06 ± 0.25 × 10 −10 g m/Pa s m 2 ) was observed in films from negro bean protein, while EF from flor de mayo bean protein exhibited the highest values of puncture strength (17.35 ± 0.82 MPa) and elongation (38.21 ± 0.64%). Most bean protein EF had reddish or brownish color; however, films from alubia and peruano bean proteins displayed light yellowish colors. FTIR spectra of EF revealed that glycerol did not react with the studied bean proteins through covalent bonds.

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Physicochemical and functional properties of kidney bean albumin and globulin protein fractions

Cited by 152 publications

References 48 publications

Structural and Functional Properties of Hemp Seed Protein Products

Structural and Functional Properties of Hemp Seed Protein Products

Effects of Red Bean (Vigna angularis) Protein Isolates on Rheological Properties of Microbial Transglutaminase Mediated Pork Myofibrillar Protein Gels as Affected by Fractioning and Preheat Treatment

Preparation and Characterization of Proteinaceous Films from Seven Mexican Common Beans (Phaseolus vulgarisL.)

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