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1.
Arch. latinoam. nutr ; 72(3): 196-204, sept. 2022. tab
Article in Spanish | LILACS, LIVECS | ID: biblio-1399277

ABSTRACT

Introduction: The use of vegetable proteins as ingredients in food systems is based on their functional properties. The water and oil holding capacity, foaming, and emulsifying capacity/stability, and antioxidant assay of the protein fractions - albumins, globulins 7S/11S, glutelins and prolamins - isolated from Leucaena seed were evaluated. Objective: The objective of this study was to evaluate the functional properties and antioxidant capacity of the concentrate and protein fractions of ripe Leucaena spp. seeds. Materials and methods: Ripe Leucaena seeds were collected and evaluated in Oaxaca, Mexico (16°59'21''N 96°43'26''O) during the months of February-April 2021.The protein concentrate was isolated by isoelectric precipitation (pH=9, pH=4). The albumins, globulins, glutelins and prolamins were isolated based on their solubility properties in different extracting solutions. Results: Glutelins constituted the main protein fraction (75.88%). Prolamins were not found. The glutelins fractions showed the highest oil holding capacity (0.93±0.08 mL g-1). The albumins fraction had the highest water holding capacity (2.53±0.15 mL g-1), foaming capacity and foam stability (71.83±1.26 % and 70.00±0.00%, respectively) and antioxidant capacity (18.09±0.88%). The globulins exhibited the highest emulsifying capacity and emulsion stability (56.83±1.76% and 55.67±1.20%, respectively). Conclusions: The concentrate and protein fraction of Leucaena seeds showed different techno-functional and antioxidant properties of interest for the food industry, like those showed by other commercial vegetable proteins(AU)


Introducción: El uso de proteínas vegetales como ingredientes en sistemas alimentarios se basa en sus propiedades funcionales. Se evaluó la capacidad de retención de agua y aceite, la capacidad/estabilidad espumante y emulsionante y el ensayo antioxidante de las fracciones proteicas -albúminas, globulinas 7S/11S, glutelinas y prolaminas- aisladas de las semillas de Leucaena. Objetivo: El objetivo de este estudio fue evaluar las propiedades funcionales y la capacidad antioxidante del concentrado y las fracciones proteicas de las semillas maduras de Leucaena spp. Materiales y métodos: Las semillas maduras de Leucaena fueron recolectadas y evaluadas en Oaxaca, México (16°59'21''N 96°43'26''O) durante los meses de febrero-abril del año 2021. Se usó harina de Leucaena desgrasada para la preparación de las fracciones proteicas. El concentrado proteico se aisló por precipitación isoeléctrica (pH=9, pH=4). Las albúminas, globulinas, glutelinas y prolaminas se aislaron en función de sus propiedades de solubilidad en diferentes soluciones de extracción. Resultados: Las glutelinas constituyeron la principal fracción proteica (75,88%). No se encontraron prolaminas. La fracción de glutelinas mostró la mayor capacidad de retención de aceite (0.93±0,08 mL g-1). La fracción de albúminas presentó la mayor capacidad de retención de agua (2,53±0,15 mL g-1), capacidad espumante y estabilidad de la espuma (71,83±1,26% y 70,00±0,00%, respectivamente) y capacidad antioxidante (18,09±0,88%). Las globulinas mostraron la mayor capacidad emulsionante y estabilidad de la emulsión (56,83±1,76 y 55,67±1,20%, respectivamente). Conclusiones: El concentrado y las fracciones proteicas de las semillas de Leucaena mostraron diferentes propiedades tecno-funcionales y antioxidantes de interés para la industria alimentaria, similares a los reportados por diversas proteínas vegetales comerciales(AU)


Subject(s)
Plant Proteins, Dietary/chemistry , Fabaceae/chemistry , Antioxidants/chemistry , Seeds , Plant Oils/chemistry , Water/chemistry , Food Industry , Albumins/chemistry , Emulsions/chemistry , Globulins/chemistry , Glutens/chemistry
2.
Indian J Biochem Biophys ; 1998 Jun; 35(3): 189-92
Article in English | IMSEAR | ID: sea-28176

ABSTRACT

An allergenic protein fraction was isolated from wheat gluten by ion exchange and gel filtration chromatography. On sodium dodecyl sulphate gel electrophoresis the molecular mass of the protein was found to be 65 kDa. By Western blotting it was confirmed that the 65 kDa protein was the major allergenic fraction causing dermatitis herpetiformis (DH) and it contained glutamic acid and proline as the major amino acids.


Subject(s)
Allergens/chemistry , Amino Acids/analysis , Chromatography , Dermatitis Herpetiformis/etiology , Electrophoresis, Polyacrylamide Gel , Glutens/chemistry , Plant Proteins/chemistry , Triticum/immunology
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