Enhancing the Usability of Pea Protein Isolate in Food Applications through Modifying Its Structural and Sensory Properties via Deamidation by Glutaminase

Abstract

This study aimed to demonstrate the feasibility of improving the properties of pea protein isolate (PPI) related to food applications via deamidation with glutaminase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FT-IR) profiling revealed that the current glutaminase treatment did not change the basic protein subunit composition. However, it allowed a certain extent of protein unfolding and conformational reorganization to generate more flexible and extended proteins with reduced average particle size and more hydrophobic groups exposed. The underlying mechanisms might include the reduction of β-sheets and antiparallel β-sheets and the increase of the β-turn structure. Moreover, the treatment time was of importance. A 12 h treatment was generally better than a 24 h treatment, and PPI treated with glutaminase at 50 °C for 12 h to a degree of deamidation of 56.1% exhibited significantly improved solubility, homogeneity, dispersibility, and suspendability with reduced beany flavor, grittiness, and lumpiness (compared to those of the untreated PPI). Thus, the glutaminase treatment offers a promising approach for enhancing the usability and applicability of pea proteins.

Improving the color and functional properties of seabuckthorn seed protein with phytase treatment combined with alkaline solubilization and isoelectric precipitation

“…Our recent research 21b found that the isoelectric point of seabuckthorn seed protein occurred at pH 5.0 (PI), which explains the lowest PS around pH 5 in this study. The increase of PS at pH values > PI was also reported by Fang et al 27 It was anticipated that the reduction in the phytic acid content by the phytase treatment could increase the solubility of seabuckthorn seed proteins, as a similar result was observed in faba bean flour protein. 19 In vitro digestibility of SSR-3h and ESSR-3h samples During the 4 h gastric digestion, the digestibility of ESSR-3h (ESSR-G: from 49.82% to 55.84%) was significantly (P < 0.05) higher than that of SSR-3h (SSR-G: from 43.61% to 48.49%) (Fig.…”

Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages.

“…Chemical modification was also applied for improving the properties of pea proteins. Deamidation with glutaminase of pea protein isolates does not change the basic protein composition but enables its unfolding and conformational reorganization (Fang, Xiang, Sun-Waterhouse, Cui, & Lin, 2020). The deamidation leads to pea proteins with higher flexibility, solubility, homogeneity and dispersibility with reduced beany flavor, grittiness, and lumpiness compared to those of the untreated.…”

“…The deamidation leads to pea proteins with higher flexibility, solubility, homogeneity and dispersibility with reduced beany flavor, grittiness, and lumpiness compared to those of the untreated. Thus, the glutaminase treatment offers a promising approach for enhancing the applicability of pea proteins (Fang et al, 2020).…”

Antihypertensive and Antioxidant Activity of Chia Protein Techno-Functional Extensive Hydrolysates

“…Currently, health-conscious consumers demand a significant increase of plant proteins consumption compared to those from animals and, consequently, an overproduction of plant proteins [5]. In line with this trend, chia is an important source of high-quality protein (19-27%), greater than traditional foods such as rice (5.95%), wheat (9.61%) and oats (13.15%) [2] and similar to other seeds used for the generation of protein isolates such as hemp [6], peas, and chickpeas [5]. Protein isolates are high-quality food ingredients with protein contents close to 90%, which can improve both the nutritional composition and techno-functional characteristics of foods.…”