Isolation and functional caharacterization of chia (Salvia hispanica) proteins

Abstract The objective was to isolate and characterize the proteins of chia seeds cultivated in the Mexican southeast. The main protein fraction was glutelins (42.94%) that had the highest Water Absorption Capacity (WAbC). Prolamins had the highest Water Adsorption Capacity (WAdC) (1.83 g/g). Glutelins registered the highest Water Holding Capacity (WHC). A higher Oil Holding Capacity (OHC) of chia protein fractions was registered in globulins and a higher Organic Molecule Absorption Capacity (OMAbC) was registered in albumin fractions (5.5 g/g of sample). At pH 2, 4 and 6, the glutelins registered a higher Emulsifying Capacity (EC) while, at pH 8 and 10, the prolamins recorded a higher EC percentage. Chia fractions registered the highest Foam Capacity (FC) values at pH 8 for globulins and pH 2 for albumins, prolamins and glutelins. Foaming and emulsifying stability (FS and ES) was greatly influenced by pH.

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Bibliographic Details
Main Author: SEGURA-CAMPOS,Maira Rubi
Format: Digital revista
Language:English
Published: Sociedade Brasileira de Ciência e Tecnologia de Alimentos 2020
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612020000200334
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Summary:Abstract The objective was to isolate and characterize the proteins of chia seeds cultivated in the Mexican southeast. The main protein fraction was glutelins (42.94%) that had the highest Water Absorption Capacity (WAbC). Prolamins had the highest Water Adsorption Capacity (WAdC) (1.83 g/g). Glutelins registered the highest Water Holding Capacity (WHC). A higher Oil Holding Capacity (OHC) of chia protein fractions was registered in globulins and a higher Organic Molecule Absorption Capacity (OMAbC) was registered in albumin fractions (5.5 g/g of sample). At pH 2, 4 and 6, the glutelins registered a higher Emulsifying Capacity (EC) while, at pH 8 and 10, the prolamins recorded a higher EC percentage. Chia fractions registered the highest Foam Capacity (FC) values at pH 8 for globulins and pH 2 for albumins, prolamins and glutelins. Foaming and emulsifying stability (FS and ES) was greatly influenced by pH.