Preparation and Characterization of Protein Isolate from Cowpea (<i>Vigna unguiculata</i> L. Walp.)

Horax, Ronny; Hettiarachchy, Navam; Chen, P.; Jalaluddin, M.

doi:10.1111/j.1365-2621.2004.tb15500.x

Cited by 46 publications

(54 citation statements)

References 24 publications

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“…(Gupta and Kapoor, 1979). On an average, legume seeds contain 20-27 per cent protein (Wang and Daun, 2004;Horax et al, 2004) and occupy the second place after cereals as the source of calories and proteins in the human diet.…”

Section: Introductionmentioning

confidence: 99%

Characterization of seed storage proteins in high protein genotypes of cowpea [Vigna unguiculata (L.) Walp.]

Gupta

Singh

Malhotra

et al. 2010

Physiol Mol Biol Plants

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Twenty one genotypes and two check varieties viz. CS-88 and V-240 of cowpea [Vigna unguiculata (L.) Walp. ] were screened for total proteins. The total protein content ranged from 22.4 (HC-3) to 27.9 % (HC-98-64) in 21 genotypes whereas in check varieties it was 25.6 (V-240) and 26.0 % (CS-88). Seven genotypes viz. HC-6, HC-5, CP-21, LST-II-C-12, CP-16, COVU-702 and HC-98-64 having high protein content (26.7 to 27.9 %) were selected for further characterization of their seed storage proteins. Globulins were the major protein fraction ranging from 55.6 (LST-II-C-12) to 58.8 % (CP-16 and HC-6) of total protein. Glutelins was the second major fraction ranging from 14.4 to 15.6 % followed by albumins (8.2 to 11.9 %) and prolamins (2.3 to 5.0 %). Content of free amino acids also showed variations amongst genotypes with COVU-702 having maximum and LST-II-C-12 having minimum content. Essential amino acid analysis revealed that S-amino acids (cysteine and methionine) were the first limiting amino acids followed by tryptophan. From the results presented here it could be suggested that two genotypes viz. LST-II-C-12 and HC-5 be used in breeding programmes aimed at developing high protein moth bean varieties with good quality.

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Section: Introductionmentioning

confidence: 99%

Characterization of seed storage proteins in high protein genotypes of cowpea [Vigna unguiculata (L.) Walp.]

Gupta

Singh

Malhotra

et al. 2010

Physiol Mol Biol Plants

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“…The ISP processing has been applied to beef and fish processing byproducts (Chen and Jaczynski 2007a;2007b;Mireles DeWitt et al 2002). Various methods of protein isolate preparation have been reported for different protein sources, including legumes (Horax et al 2004), oilseeds (Horax et al 2011), cereals (Agboola et al 2005;Ju et al 2001;Paraman et al 2007) and fish protein (Azadian et al 2012;Chanarat and Benjakul 2013) based on solubility behavior of their proteins. Proteins isolates are the basic functional components of various high protein processed food products and thus determine the textural and nutritional properties of the foods.…”

Section: Introductionmentioning

confidence: 99%

Preparation and characterization of protein isolate from Yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process

Lee

Yoon

et al. 2016

Fish Aquatic Sci

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Isoelectric solubilization/precipitation (ISP) processing allows selective, pH-induced water solubility of proteins with concurrent separation of lipids and removal of materials not intended for human consumption such as bone, scales, skin, etc. Recovered proteins retain functional properties and nutritional value. Four roe protein isolates (RPIs) from yellowfin tuna roe were prepared under different solubilization and precipitation condition (pH 11/4.5, pH 11/5.5, pH 12/4.5 and pH 12/5.5). RPIs contained 2.3-5.0 % moisture, 79.1-87.8 % protein, 5.6-7. 4 % lipid and 3.0-3.8 % ash. Protein content of RPI-1 and RPI-2 precipitated at pH 4.5 and 5.5 after alkaline solubilization at pH 11, was higher than those of RPI-3 and RPI-4 after alkaline solubilization at pH 12 (P < 0.05). Lipid content (5.6-7.4 %) of RPIs was lower than that of freeze-dried concentrate (10.6 %). And leucine and lysine of RPIs were the most abundant amino acids (8.8-9.4 and 8.5-8.9 g/100 g protein, respectively). S, Na, P, K as minerals were the major elements in RPIs. SDS-PAGE of RPIs showed bands at 100, 45, 25 and 15 K. Moisture and protein contents of process water as a 2'nd byproduct were 98.9-99.0 and 1.3-1.8 %, respectively. Therefore, yellowfin tuna roe isolate could be a promising source of valuable nutrients for human food and animal feeds.

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“…Thus, the commercial applications in food industry have been limited mostly to soybean and milk proteins. Recently, the increased demand to plant based proteins as food ingredients has also encouraged studies on functionality of proteins from soybean alternative legumes such as chickpeas, common beans, lentils, cowpeas, lupins, peas and broad beans (Bamdad, Goli, & Kadivar, 2006;Horax, Hettiarachchy, Chen, & Jalaluddin, 2004;Makri, Papalamprou, & Doxastakis, 2005;Morales-De Leon, Vazquez-Mata, Torres, Gil-Zenteno, & Bressani, 2007;Sanchez-Vioque, Clemente, Vioque, Bautista, & Millan, 1999). However, there are very limited studies related to antioxidant activity of soybean alternative legume proteins.…”

Section: Introductionmentioning

confidence: 99%

Effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea proteins

Arcan

Yemenicioğlu

2010

Food Research International

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a b s t r a c tThis study investigated the effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea protein extracts (CPE). The enzyme hydrolysis increased soluble protein content (1.2 to 2-fold) and free radical scavenging activity (1.9 to 3-fold) of hydrolyzed chickpea protein extract (HCPE), but almost unaffected its antioxidant potential in oil-in-water emulsion system and reduced its iron chelating capacity (1.3-fold) and functional properties. The chromatographic fractions of CPE are mainly acidic, while those of HCPE are mainly basic and neutral. The majority of chickpea proteins had pI between 4.5 and 5.5, and molecular weight (MW) between 15 and 40 kDa, while MW of their pepsin hydrolysis products ranged between 6.5 and 14.2 kDa. The main antioxidant proteins in CPE and HCPE fractionated by ultrafiltration had MW greater than 30 kDa and between 2 and 10 kDa, respectively. The chickpea proteins and hydrolysates showed different potentials as functional food ingredients.

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Preparation and Characterization of Protein Isolate from Cowpea (Vigna unguiculata L. Walp.)

Cited by 46 publications

References 24 publications

Characterization of seed storage proteins in high protein genotypes of cowpea [Vigna unguiculata (L.) Walp.]

Characterization of seed storage proteins in high protein genotypes of cowpea [Vigna unguiculata (L.) Walp.]

Preparation and characterization of protein isolate from Yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process

Effects of controlled pepsin hydrolysis on antioxidant potential and fractional changes of chickpea proteins

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