气候变化领域集成服务门户(CCPortal): Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions

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DOI	10.1007/s11130-020-00871-7
	Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions
	Fernández Sosa E.I.; Chaves M.G.; Quiroga A.V.; Avanza M.V.
发表日期	2021
ISSN	9219668
起始页码	37
结束页码	45
卷号	76 期号:1
英文摘要	Pigeon pea protein isolates (PPI) are an option to obtain a high yield of good quality proteins and represent a great potential for the food industry. In this work, physicochemical and structural properties of albumin (ALB), globulin (GLB), and PPI obtained at different pHs (8, 9, 10, and 11) were studied to deepen the knowledge of these proteins for future application. GLB presented protein aggregates and polypeptides characteristics of 7S vicilin subunits while ALB presented polypeptides with low molecular masses. GLB showed a more compact and less flexible structure than ALB fraction due to the distinct conformational characteristics found in DSC, fluorescence spectroscopy, Ho. These structural characteristics conferred GLB greater conformational stability (∆GH2O) than ALB fraction. The latter presented a higher proportion of β-strand in aggregated structures. PPI11 showed the highest protein recovery, but the least So with more presence of protein aggregates with the least proportion of β-strands in aggregated structures. A higher percentage of protein unfolding and exposure of hydrophobic residues to solvent was observed as the extraction pH of the isolates increased. Enthalpy change of transition decreased, and the maximum emission wavelength shifted to red in fluorescence spectroscopy. However, PPI11 showed only a slight increase in Ho (10%) with respect to PPI8. The variation in pH for protein extraction constitutes a simple, rapid, and low-cost method to obtain PPI with physicochemical and structural properties that will determine its functional properties and their use as food ingredients. © 2020, The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature.
英文关键词	Albumin; Free energy of denaturation; FTIR; Globulin; Hydrophobicity; SEC
scopus关键词	globulin; peptide; animal; Cajanus; Columbidae; pea; Animals; Cajanus; Columbidae; Globulins; Peas; Peptides
来源期刊	Plant Foods for Human Nutrition
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/177232
作者单位	Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste (UNNE) and Instituto de Química Básica y Aplicada del Nordeste Argentino (IQUIBANEA) UNNE-CONICET, Avenida Libertad 5470, Corrientes, 3400, Argentina; Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA) UNLP-CONICET, 47 y 116, La Plata, 1900, Argentina
推荐引用方式 GB/T 7714	Fernández Sosa E.I.,Chaves M.G.,Quiroga A.V.,et al. Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions[J],2021,76(1).
APA	Fernández Sosa E.I.,Chaves M.G.,Quiroga A.V.,&Avanza M.V..(2021).Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions.Plant Foods for Human Nutrition,76(1).
MLA	Fernández Sosa E.I.,et al."Comparative Study of Structural and Physicochemical Properties of Pigeon Pea (Cajanus cajan L.) Protein Isolates and its Major Protein Fractions".Plant Foods for Human Nutrition 76.1(2021).