Dry fractionated faba bean protein-rich flour (FPR) produced by milling/air classification, and faba bean protein isolate (FPI) produced by acid extraction/isoelectric precipitation were compared in terms of composition, techno-functional properties, nutritional properties and environmental impacts. FPR had a lower protein content (64.1%, dry matter (DM)) compared to FPI (90.1%, DM), due to the inherent limitations of air classification. Of the two ingredients, FPR demonstrated superior functionality, including higher protein solubility (85%), compared to FPI (32%) at pH 7. Foaming capacity was higher for FPR, although foam stability was similar for both ingredients. FPR had greater gelling ability compared to FPI. The higher carbohydrate content of FPR may have contributed to this difference. An amino acid (AA) analysis revealed that both ingredients were low in sulfur-containing AAs, with FPR having a slightly higher level than FPI. The potential nutritional benefits of the aqueous process compared to the dry process used in this study were apparent in the higher in vitro protein digestibility (IVPD) and lower trypsin inhibitor activity (TIA) in FPI compared to FPR. Additionally, vicine/convicine were detected in FPR, but not in FPI. Furthermore, much lower levels of fermentable oligo-, di- and monosaccharides, and polyols (FODMAPs) were found in FPI compared to FPR. The life cycle assessment (LCA) revealed a lower environmental impact for FPR, partly due to the extra water and energy required for aqueous processing. However, in a comparison with cow’s milk protein, both FPR and FPI were shown to have considerably lower environmental impacts.

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Similarly prepared protein isolates from blue lupin (Lupinus angustifolius) and white lupin (L. albus) were assessed in relation to their composition, functional properties, nutritional attributes and environmental impacts. Blue lupin protein isolate (BLPI) and white lupin protein isolate (WLPI) were found to be quite similar in composition, although differences in the electrophoretic protein profiles were apparent. Both lupin protein isolates (LPIs) had good protein solubility (76.9% for BLPI and 69.8% for WLPI at pH 7) and foaming properties. However, a remarkable difference in heat gelation performance was observed between BLPI and WLPI. WLPI had a minimum gelling concentration of 7% protein, whereas BLPI required 23% protein in order to form a gel. WLPI also resulted in stronger gels over a range of concentrations compared to BLPI. Nutritional properties of both LPIs were similar, with no significant differences in in vitro protein digestibility (IVPD), and both had very low trypsin inhibitor activity (TIA) and fermentable oligo-, di- and monosaccharides, and polyols (FODMAP) content. The amino acid profiles of both LPIs were also similar, with sulfur-containing amino acids (SAAs) being the limiting amino acid in each case. Environmental impacts revealed by the life cycle assessment (LCA) were almost identical for BLPI and WLPI, and in most categories the LPIs demonstrated considerably better performance per kg protein when compared to cow’s whole milk powder.

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Pulse proteins are being increasingly investigated as nutritious and functional ingredients which could provide alternatives to animal proteins; however, pulse protein ingredients do not always meet the functionality requirements necessary for various applications. Consequently, enzymatic hydrolysis can be employed as a means of improving functional properties such as solubility, emulsifying, foaming, and gelling properties. This review aims to examine the current literature regarding modification of these properties with enzymatic hydrolysis. The effects of enzymatic hydrolysis on the functionality of pulse proteins generally varies considerably based on the enzyme, substrate, processing steps such as heat treatment, degree of hydrolysis, and pH. Differences in protease specificity as well as protein structure allow for a wide variety of peptide mixtures to be generated, with varying hydrophobic and electrostatic properties. Typically, the most significant improvements are seen when the original protein ingredient has poor initial functionality. Solubility is usually improved in the mildly acidic range, which may also correspond with improved foaming and emulsifying properties. More work should be carried out on the potential of enzymatic hydrolysis to modify gelation properties of pulse proteins, as the literature is currently lacking. Overall, careful selection of proteases and control of hydrolysis will be necessary to maximize the potential of enzymatic hydrolysis as a tool to improve pulse protein functionality and broaden the range of potential applications.

The effects of hydrolysis by commercial food-grade proteases on the physicochemical and techno-functional properties of lentil protein concentrate were investigated. Lentil protein concentrate was hydrolysed with Alcalase, Novozym 11028 or Flavourzyme, and a control was prepared without enzyme addition under the same conditions. Differences in specificity between the three proteases were evident in the electrophoretic protein profile, reversed-phase HPLC peptide profile, and free amino acid composition. Alcalase and Novozym were capable of extensively degrading all the major protein fractions. Alcalase or Novozym treatment resulted in considerably higher solubility under acidic conditions compared to the control. Flavourzyme treatment resulted in moderately improved solubility in the acidic range, but slightly lower solubility at pH 7. Alcalase treatment resulted in slightly larger particle size and slightly higher viscosity. The foaming properties of the protein concentrate were not significantly affected by hydrolysis. Increased solubility in acidic conditions with hydrolysis could broaden the range of food and beverage applications for lentil protein concentrate.

BACKGROUND: Plant-based milk alternatives are becoming more popular. However, many are low in nutrients, particularly protein. More attention is being given to plant protein isolates / concentrates as potential ingredients in high-protein milk alternative formulations. RESULTS:The effect of lupin protein source on the physicochemical, functional, and nutritional characteristics of model milk alternatives was investigated. Milk alternatives were produced with either blue lupin or white lupin protein isolate, formulated to contain similar levels of protein and fat as low-fat cow's milk. Nutritional composition and predicted glycemic properties were measured. The effect of homogenization pressure on the physicochemical properties and storage stability was also assessed, with cow's milk and soy milk alternative analyzed for comparison. Both blue and white lupin milk alternatives were high in protein, low in fermentable oligo-, di-and monosaccharides, and polyols (FODMAPs), and had a low predicted glycemic index. White lupin milk alternatives had smaller particle size as well as greater stability, with less creaming compared to blue lupin milk alternatives, although the former showed slightly higher sediment layers. Increasing homogenization pressure from 180 to 780 bar resulted in smaller particle size, lower separation rate, and greater foamability for both blue and white lupin milk alternatives. White lupin milk alternative homogenized at 780 bar was found to be the most stable product, with a similar separation rate to cow's milk.CONCLUSIONS: These results indicate that protein source and processing can influence functional properties significantly along with product stability, and this is an important consideration when formulating high-protein milk alternatives.