Enzymatic modification of rice bran protein: Impact on structural, antioxidant and functional properties

Antioxidant Activity, Functional Properties, and Cytoprotective Effects on HepG2 Cells of Tree Peony (Paeonia suffruticosa Andr.) Seed Protein Hydrolysate as Influenced by Molecular Weights Fractionation

“…The lower EAI of TPSPH and five fractions at pH 3.0 and 5.0 might be due to the protein molecules’ aggregation at pH 3.0 and 5.0, close to the isoelectric point of tree peony seed protein, reducing the protein adsorption at the oil–water interface [ 2 ]. Singh et al [ 25 ] also reported that rice bran protein hydrolysates with different degrees of hydrolysis had low EAI near their isoelectric point pH 5.0. As the pH increased from 7.0 to 9.0, the EAI values of TPSPH and five fractions increased from 9.95 m 2 /g to 192.69 m 2 /g.…”

“…The EAI values of MW > 30 kDa increased from 60.63 m 2 /g to 192.69 m 2 /g with an increasing pH of 5.0 to 9.0, which was significantly higher than those of low-MW fractions (9.95–72.24 m 2 /g) ( p < 0.05). Similarly, high-MW peptide of rice bran protein hydrolysates (23.4–44.5 m 2 /g) also exhibited stronger emulsifying properties than low-MW peptides (17.7–34.4 m 2 /g) at pH 5.0 to 9.0 [ 25 ]. It is reported that the EAI of protein/peptide was principally related to surface hydrophobicity and molecular weight [ 27 ].…”

Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients

“…As a result, the PDCAAS of the hydrolysate was also higher, compared to the original ingredient. Similarly, for progressively higher degrees of hydrolysis, a papain–hydrolysate of rice bran PC was more extensively digested than the intact PI by pepsin–pancreatin digestion [ 56 ].…”

“…The following supporting information can be downloaded at: , Table S1: Summary of digestion assays, sample treatment and measurement from studies investigating the effect of processing on protein digestion. References [ 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 ,…”

Multifaceted functionality of l-arginine in modulating the emulsifying properties of pea protein isolate and the oxidation stability of its emulsions

“…The modification technology of plant proteins can be divided into three categories: physical modification, chemical modification and enzymatic modification. [6][7][8][9] Physical modification ensures product safety; however, the impact of this treatment is not always evident. Although the effect of acid-base treatment can be significant, it may cause nutrient loss and introduce reagent residues.…”