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.

A study to determine the protein digestibility‐corrected amino acid score and protein efficiency ratio of nine different cooked Canadian pulse classes was conducted in support of the establishment of protein quality claims in Canada and the United States. Split green and yellow pea, whole green lentil, split red lentil, Kabuli chickpea, navy bean, pinto bean, light red kidney bean, and black bean were investigated. Protein digestibility‐corrected amino acid score (PDCAAS) and the protein efficiency ratio (PER) were determined using the appropriate rodent models. All pulses had high digestibility values, >70%, with PDCAAS values greater than 0.5, thereby qualifying as a quality protein in the United States, but only navy beans qualified as a good source of protein. All pulses except whole green lentils, split red lentils, and split green peas would qualify as sources of protein with protein ratings between 20 and 30.4 in Canada. These findings support the use of pulses as protein sources in the regulatory context of both the United States and Canada.

In this work, the protein quality of different bean types after undergoing the preparatory methods of baking, cooking and extrusion was assayed. Protein quality was assessed using a rodent bioassay to evaluate growth and protein digestibility while amino acid composition was determined via HPLC. In vivo protein digestibility was compared to an in vitro assessment method. The average protein digestibility corrected amino acid score (PDCAAS) for processed beans was higher than the digestible indispensable amino acid score (DIAAS) (61% vs. 45%). Extrusion/cooking of Phaseolus varieties resulted in higher PDCAAS (66% on average) and DIAAS values (61% on average) than baked (52% and 48%) while baked faba beans had higher PDCAAS (66%) and DIAAS (61%) values. A significant correlation was found between PDCAAS and in vitro PDCAAS (R² = 0.7497). This demonstrates which bean processing method will generate the optimal protein quality, which has benefits for both industrial production and individual domestic preparation.