Food proteins: a review on their emulsifying properties using a structure-function approach.

Carrageenan and its applications in drug delivery.

In keeping with emerging consumer trends, the food industry is continually searching for cheaper and healthier protein ingredients to replace those derived from animal sources (e.g., whey, casein, gelatin, and ovalbumin), gluten-based proteins (e.g., wheat), and soy. Pea protein shows promise in filling this niche because it is non-genetically modified organism (GMO), gluten-free, nutritious, and of low allergenicity. This review discusses structure–function relationships of pea protein isolates, the impact of extraction techniques used to produce the isolate, and the impact of cultivar and environment on ingredient performance in terms of solubility, water- and oil-holding capacities, emulsifying, foaming, and gelation properties.

Pea protein isolates: Structure, extraction, and functionality

This is psychology

The interactions of proteins and polyelectrolytes lead to diverse applications in separations, delivery and wound repair, and are thus of interest to scientists in e.g. (a) glycobiology, (b) tissue engineering, (c) biosensing, and (d) pharmacology. This breadth is accompanied by an assortment of contexts and models in which polyelectrolytes are seen as (a) protein cognates assisting in complex cellular roles, (b) surrogates for the extracellular matrix, mimicking its hydration, mechanical and sequestering properties, (c) benign hosts that gently entrap, deposit and tether protein substrate specificity, and (d) selective but non-specific agents that modify protein solubility. Unsurprisingly, this literature is somewhat segregated by objectives and paradigms. We hope this review, which emphasizes publications over the last 8 years, represents and also counterbalances that divergence. An ongoing theme is the role of electrostatics, and we show how this leads to the variety of physical forms taken by protein–polyelectrolyte complexes. We present approaches towards analysis and characterization, motivated by the goal of structure–property elucidation. Such understanding should guide in applications, our third topic. We present recent developments in modeling and simulations of protein–polyelectrolyte systems. We close with a prospective on future developments in this field.

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Protein–polyelectrolyte interactions

Functional attributes of pea protein isolates prepared using different extraction methods and cultivars

Formation and functionality of whey protein isolate–(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes

Complex coacervation of pea protein isolate and alginate polysaccharides

In order to determine the impact of fermentation on protein quality, pea protein concentrate (PPC) was fermented with Lactobacillus plantarum for 11 h and total phenol and tannin contents, protease inhibitor activity, amino acid composition and in vitro protein digestibility were analyzed. Phenol levels, expressed as catechin equivalents (CE), increased on dry mass basis from 2.5 at 0 h to 4.9 mg CE per 1 g of PPC at 11 h. Tannin content rose from 0.14 at 0 h to a maximum of 0.96 mg CE per 1 g of PPC after 5 h, and thereafter declined to 0.79 mg/g after 11 h. After 9 h of fermentation trypsin inhibitor activity decreased, however, at all other fermentation times similar levels to the PPC at time 0 h were produced. Chymotrypsin inhibitor activity decreased from 3.7 to 1.1 chymotrypsin inhibitory units (CIU) per mg following 11 h of fermentation. Protein digestibility reached a maximum (87.4%) after 5 h of fermentation, however, the sulfur amino acid score was reduced from 0.84 at 0 h to 0.66 at 11 h. This reduction in sulfur content altered the in vitro protein digestibility-corrected amino acid score from 67.0% at 0 h to 54.6% at 11 h. These data suggest that while fermentation is a viable method of reducing certain non-nutritive compounds in pea protein concentrate, selection of an alternative bacterium which metabolises sulfur amino acids to a lesser extent than L. plantarum should be considered.

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Effect of Fermentation on the Protein Digestibility and Levels of Non-Nutritive Compounds of Pea Protein Concentrate.

Surface characteristics and functional attributes of protein isolates prepared from different pea cultivars using isoelectric precipitation were investigated. Protein levels of isolates ranged from 81–89% with isoelectric points occurring between pH 4.7–4.9. Surface hydrophobicity values differed among cultivars with CDC Dundurn and CDC Striker isolates having the lowest and highest values, respectively. Protein solubility values at pH 7.0 varied with MFR042 and CDC Dundurn isolates displaying the lowest (approximately 54%) and highest (approximately 76%) values, respectively. No significant (p>0.05) differences existed between cultivar isolates for water hydration and oil holding capacity values. Cooper and CDC Dundurn isolates had significantly (p<0.05) lower emulsifying activity indices (EAI) (approximately 31–33 m2/g) than the other cultivars. Emulsifying stability index values were all similar. EAI values were positively correlated with surface hydrophobicity values and negatively correlated with solubility values. Varietal differences for the functional attributes of solubility and emulsification were identified.

Andrea K. Stone

Papers

Functional attributes of pea protein isolates prepared using different extraction methods and cultivars

Formation and functionality of whey protein isolate–(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes

Complex coacervation of pea protein isolate and alginate polysaccharides

Effect of Fermentation on the Protein Digestibility and Levels of Non-Nutritive Compounds of Pea Protein Concentrate.

Functional properties of protein isolates from different pea cultivars