Abstract

Combinations of enzymatic hydrolysis using different proteolytic enzymes (papain, Esperase®, trypsin) and lactic fermentation with Lactobacillus plantarum were used to alter potential pea allergens, the functional properties and sensory profile of pea protein isolate (PPI). The order in which the treatments were performed had a major impact on the changes in the properties of the pea protein isolate; the highest changes were seen with the combination of fermentation followed by enzymatic hydrolysis. SDS-PAGE, gel filtration, and ELISA results showed changes in the protein molecular weight and a reduced immunogenicity of treated samples. Treated samples showed significantly increased protein solubility at pH 4.5 (31.19–66.55%) and at pH 7.0 (47.37–74.95%), compared to the untreated PPI (6.98% and 40.26%, respectively). The foaming capacity was significantly increased (1190–2575%) compared to the untreated PPI (840%). The treated PPI showed reduced pea characteristic off-flavors, where only the treatment with Esperase® significantly increased the bitterness. The results from this study suggest that the combination of enzymatic hydrolysis and lactic fermentation is a promising method to be used in the food industry to produce pea protein ingredients with higher functionality and a highly neutral taste. A reduced detection signal of polyclonal rabbit anti-pea-antibodies against the processed protein preparations in ELISA furthermore might indicate a decreased immunological reaction after consumption.

Highlights

  • Peas (Pisum sativum L.) are increasingly used due to their sustainable production [1], economic benefits [2], high protein content (15–30%), and alleged low allergenicity

  • This study aimed to investigate the effects of combining enzymatic hydrolysis and fermentation on allergenic proteins (Pis s1 and Pis s2), as measured by SDS-PAGE and the ability of polyclonal sera to recognize antigens, functional properties and on the debittering and characteristic off-flavors of pea proteins

  • Fermentation of pea protein isolate (PPI) hydrolysates resulted in significantly higher viable cell counts compared to the fermented PPI

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Summary

Introduction

Peas (Pisum sativum L.) are increasingly used due to their sustainable production [1], economic benefits [2], high protein content (15–30%), and alleged low allergenicity. They belong to the legume family (Fabaceae) and their proteins are classified as salt-, water-, and ethanol soluble, corresponding to globulins, albumins, and prolamins, respectively [3]. The allergen Pis s1 correspond to the mature vicilin (47–50 kDa) as well as to one of vicilin’s proteolytic fractions (32 kDa). Pea allergens have shown homology between epitopes (recognition sites) from other legume allergens [7] and serological cross-reactivity has been proved [4,8,9]

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