Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction

Liu, Yan; Zhao, Guanli; Zhao, Ming; Ren, Jiaoyan; Yang, Bao

doi:10.1016/j.foodchem.2011.09.074

Cited by 226 publications

(155 citation statements)

References 33 publications

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“…The local variety Chounfakhi can produce an appreciable quantity of protein, which encourages its cultivation in regions where it can adapt to climatic and edaphic conditions. Compared to other plant proteins, especially commercial soy protein isolate, the functional properties of peanut proteins were much poorer, which might greatly limit the application of peanut proteins in many food formulations (Liu et al, 2012). Using adequate buff ers, we isolated all protein classes in seeds of the four varieties and found that they were almost totally composed of globulins (95%), albumins, prolamins, and glutelins being with negligible contents (Table 1).…”

Section: Biochemical Compositionmentioning

confidence: 99%

Lipids, proteins, phenolic composition, antioxidant and antibacterial activities of seeds of peanuts (Arachis hypogaea l) cultivated in Tunisia

et al. 2013

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Fatty acid composition of peanut seed oil in four varieties cultivated in Tunisia showed that linoleic (C18:2), oleic (C18:1) and palmitic (C16) acids account for more than 84% for Chounfakhi and Massriya and for more than 85% of the total fatty acids of Trabilsia and Sinya seed oil respectively. Seed oil contents were signifi cantly diff erent (P ≤ 0.05) and did not exceed 48%. The study of total phenolics revealed that Chounfakhi contained more total phenolics (2.1 mg GAE/g DW), followed by the Massriya and Sinya cultivars (1.35 mg GAE/g DW for each); Trabilsia presented the lowest total phenolic content with 1 mg GAE/g DW. Considerable antiradical ability was found, especially in the Trabilsia peanut seed cultivar (IC50 = 1550 μg/ml), the Massriya and Sinya cultivars had, respectively, 720 and 820 mg/ml IC50. In the Massriya variety the sterol fraction showed antibacterial activity against Listeria ivanovii, Listeria inocua, Pseudomonas aeruginosa, Staphylococus aureus, Enterococcus hirae and Bacillus cereus.

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Section: Biochemical Compositionmentioning

confidence: 99%

Lipids, proteins, phenolic composition, antioxidant and antibacterial activities of seeds of peanuts (Arachis hypogaea l) cultivated in Tunisia

et al. 2013

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“…In the food industry, soybean protein has wide range of applications especially in the processed foods (meat, milk, beverage, and bakery products), due to its nutritional and functional benefits (Liu 1999). The functional properties of proteins such as solubility, gelation, emulsification, foaming, and viscosity play a major role in the food systems.…”

Section: Introductionmentioning

confidence: 99%

Improved functional properties of glycosylated soy protein isolate using D-glucose and xanthan gum

Hettiarachchy

Rayaprolu

et al. 2015

J Food Sci Technol

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Functional properties of the soy protein need to improve to have better applications in food industry. Alkali extracted and acid precipitated soy protein isolate (SPI) was glycosylated using D-glucose (G) and Xanthan gum (X) via Maillard reaction to improve solubility. The effects of SPI to G and SPI to X ratios (SPI:G = 2:1, 1:1, and 1:2; SPI:X = 100:1 and 10:1) and incubation time (0, 6, 12, and 24 h) on the solubility and functional properties of glycosylated SPI were evaluated. The SPI:G ratio of 1:2 yielded a maximum degree of glycosylation of 71.1 %. The solubility of SPI after glycosylation significantly increased (P<0.05) at pH 4.0-8.0 compared to SPI alone. Although the emulsion stability of glycosylated SPIs has not significantly increased (P>0.05), the emulsifying activity improved significantly (P<0.05). Glycosylation with SPI-X at a ratio of 10: 1 showed maximum emulsifying activity of 191.6 m 2 /g (SPI alone: 66.3 m 2 /g). Moreover, the SPI:X (ratio of 100:1) showed the maximum foaming activity (205 mL) compared to SPI alone (155 mL). The foaming stability of SPI (2.6 %) increased to 5.5 and 8.2 % when using xanthan gum at the ratio of 100:1 and 10:1, respectively. Glycosylated SPI with enhanced emulsifying and foaming properties has potential to improve the functional quality of the food products.

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“…SDS-PAGE analysis has been used to investigate glycated proteins in two past studies (Diftis & Kiosseoglou, 2006;Liu, Zhao, Zhao, Ren, & Yang, 2012). Chemical features of GC-SPI in the present study were also revealed by this technique.…”

Section: Preparation and Analyses Of Gc-spimentioning

confidence: 53%

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Zhu

Liu

et al. 2015

CyTA - Journal of Food

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Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan Cambios en la estructura y en las propiedades del aislado de proteína de soja como resultado de la glicación y reticulación mediante transglutaminasa y chitosán degradado A glycated and cross-linked soybean protein isolate (GC-SPI) with the glucosamine content of 19.40 g/kg protein was prepared by using SPI, transglutaminase, and a degraded chitosan under fixed conditions, aiming to assess modified properties and potential application of GC-SPI. GC-SPI has less reactable -NH 2 groups than SPI (0.38 versus 0.48 mol/kg protein), and is verified by electrophoretic analysis to be a glycated and cross-linked protein product. Infrared spectroscopy and circular dichroism analyses demonstrate that GC-SPI contains more -OH groups, and has a more open secondary structure. In comparison with SPI, GC-SPI has higher surface hydrophobicity but lower in vitro digestibility due to protein cross-linking, and exhibits greater water-and oil-binding capacities (9.9 versus 6.4 and 3.7 versus 2.0 kg/kg protein). It is concluded that the glycation and cross-linking confer an open structure and modified properties of SPI, and GC-SPI is a potential ingredient with better hydration and oil-binding than SPI.Keywords: soybean protein isolate; degraded chitosan; transglutaminase; secondary structure; property Se preparó aislado de proteína de soja glicada y reticulada (GC-SPI) con un contenido de glucosamina de 19,40 g/kg de proteína utilizando SPI, transglutaminasa y chitosán degradado sometido a condiciones determinadas con el objetivo de estudiar las propiedades modificadas y las aplicaciones potenciales de GC-SPI. GC-SPI obtuvo menos grupos reactivos de tipo NH 2 en comparación con SPI (0,38 frente a 0,48 mol/kg de proteína) y se verificó mediante análisis electroforético para ser un producto proteínico glicado y reticulado. La espectroscopía infrarroja y el análisis de dicroísmo circular mostraron que el GC-SPI contiene más grupos OH y tiene una estructura secundaria más abierta. En comparación con SPI, GC-SPI tiene una mayor superficie de hidrofobia aunque una menor digestibilidad in vitro debido a la reticulación proteínica, además exhibe una mayor capacidad de retención de agua y de aceite (9,9 frente a 6,4 y 3,7 frente a 2,0 kg/kg de proteína). En conclusión, la glicación y la reticulación conceden una estructura abierta y unas propiedades modificadas en SPI. Además GC-SPI se trata de un ingrediente potencial con una mejor hidratación y capacidad de retención que SPI.Palabras clave: aislado de proteína de soja; chitosán degradado; transglutaminasa; estructura secundaria; propiedad

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Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction

Cited by 226 publications

References 33 publications

Lipids, proteins, phenolic composition, antioxidant and antibacterial activities of seeds of peanuts (Arachis hypogaea l) cultivated in Tunisia

Lipids, proteins, phenolic composition, antioxidant and antibacterial activities of seeds of peanuts (Arachis hypogaea l) cultivated in Tunisia

Improved functional properties of glycosylated soy protein isolate using D-glucose and xanthan gum

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

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