Effect of enzyme‐assisted hydrolysis on protein pattern, technofunctional, and sensory properties of lupin protein isolates using enzyme combinations

Abstract

The modification of lupin protein isolates (LPI) by means of enzymatic hydrolysis ( Lupinus angustifolius cultivar Boregine) was performed with four enzyme preparations (Alcalase 2.4 L, Papain, Corolase 7089, and Neutrase 0.8 L) in a one‐ and two‐step process to determine the efficacy for the destruction of major IgE‐reactive polypeptides and the evaluation of the technofunctional and sensory properties of lupin protein hydrolysates. Combinations of Alcalase 2.4 L and Papain were most effective in the degradation of polypeptides in L. angustifolius as measured by sodium dodecylsulfate–polyacrylamide gel electrophoresis. The enzymatic hydrolysis of the LPI increased their technofunctional properties such as protein solubility, foam activity, and emulsifying capacity almost independently of the enzyme preparation used. The sensory results showed a significant increase in bitterness from 1.9 for LPI to 5.7 for the combination of Alcalase 2.4 L and Papain in one‐step process. The aroma attributes of the hydrolysates were very similar to untreated LPI. The results of this study show the possibility of enzymatic hydrolysis of LPI to destroy the major IgE‐reactive polypeptides that increase the technofunctional properties of the isolates and thus their use in human nutrition as food ingredients.

Use of Alcalase in the production of bioactive peptides: A review

“…The 10% hydrolysate was the best concentration in terms of nutritional parameters and sensory scores [735], later this product was remarked as a functional food [736]. Corolase, papain, Alcalase and Neutrase were individually used or in a two-step process to hydrolyze lupin (Lupinus angustifolius cultivar Boregine) protein isolates [737].…”

Fermentation of Lupin Protein Hydrolysates—Effects on Their Functional Properties, Sensory Profile and the Allergenic Potential of the Major Lupin Allergen Lup an 1

“…Alcalase 2.4 L hydrolysates are known for bitter taste. Several studies have already shown that the hydrolysis of plant proteins such as lupin [ 7 , 10 ], soy [ 6 ] and pea [ 27 ] results in a bitter taste. However, S4 ( Lactobacillus sakei ssp .…”

“…Unfermented LPI (−0.896/−1.108) was in close correlation with the pea-like aroma attribute and was found on the negative side of PC2, together with the Papain hydrolysates samples S1 (Lactobacillus sakei ssp. carnosus) and S3 (Lactobacillus helveticus) and the Alcalase 2.4 L hydrolysates samples S5 (Lactobacil- [7,10], soy [6] and pea [27] results in a bitter taste. However, S4 (Lactobacillus sakei ssp.…”

“…However, the use of lupin proteins in some foods like refreshing drinks is limited due to the characteristics of their functional properties, in particular their solubility in the acidic range. Several studies have shown that enzymatic hydrolysis can significantly improve the functional properties of plant proteins such as protein solubility, foaming and emulsification [ 5 , 6 , 7 , 8 , 9 , 10 ]. In addition, it was shown that the allergenicity of the proteins can be reduced by enzymatic treatments [ 11 , 12 ].…”

Plant Proteins for Future Foods: A Roadmap

“…Zang et al explained that the release of soluble peptides from insoluble aggregates or precipitates, and an increased number of exposed ionizable amino and carboxyl groups, were the reasons behind the increased protein solubility and DH [153]. Schlegel et al reported that lupin protein hydrolysates showed a significant increase in foaming activity, as compared to the native sample [156]. The increase in foaming activity was a result of the change in protein structure, which exposed the hydrophilic and polar groups to interactions with an aqueous environment.…”