Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer

Jarpa‐Parra, Marcela; Bamdad, Fatemeh; Tian, Zhigang; Zeng, Hongbo; Temelli, Feral; Chen, L.

doi:10.1016/j.colsurfb.2015.04.065

Cited by 139 publications

(75 citation statements)

References 29 publications

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“…Foaming capacity provides a desirable and unique texture to a range of aerated foods including ice-cream, bread, and cakes. In this study, faba bean protein showed poor foaming properties with the FC value of 31.2% at pH 5 and 66.7% at pH 7 (Figure 4a), which are lower than those reported for pea (167.4%-243.7%) and lentil proteins (403%-425%) (Jarpa-Parra et al, 2015;Lam et al, 2017). This is directly related to the low solubility of faba bean protein (Vioque et al, 2012).…”

Section: Evaluation Of Functional Propertiescontrasting

confidence: 64%

Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein

et al. 2019

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Background and objectives Faba bean proteins isolates did not show sufficient functional properties for food applications due to poor solubility. Enzymatic treatments and ultrafiltration may improve solubility and functional properties of faba bean protein. The aim of the present work was to investigate the effect of different proteases (pepsin, trypsin, flavourzyme® 500 L, neutrase® 0.8 L), hydrolysis time and ultrafiltration technique on the physicochemical and functional characteristics of faba bean protein. Findings The protein solubility increased from 24.4% to 88.8% at pH 7 and 81.0% at pH 5 by pepsin hydrolysis (15 min). Their foaming capacity (FC) increased from 31.2% to 122.2% at pH 5 and 66.7% to 131.2% at pH 7 and the oil holding capacity (OHC) increased from 6.12 to 8.21 g/g by pepsin hydrolysis. Fraction I (Mw > 10 kDa) and II (Mw: 5–10 kDa) obtained after pepsin hydrolysis and ultrafiltration demonstrated further improved foaming and oil holding capacity and much improved emulsifying capacity. Conclusions Enzymatic hydrolysis and ultrafiltration provided a strategy to significantly improve faba bean protein solubility and functional properties. Significance and novelty Faba bean protein hydrolysates and ultrafiltration fractions are good sources of protein with excellent solubility and functionality.

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Section: Evaluation Of Functional Propertiescontrasting

confidence: 64%

Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein

et al. 2019

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“…The batter of the control angel food cake (AC‐0‐LPC) had the lowest specific gravity (0.33 g L −1 ), while this value increased significantly with the increasing amount of lentil protein in the formulation ( P < 0.05), indicating less air being incorporated into the batter (Campbell et al ., ). Lentil protein possesses good foaming capacity due to the balanced hydrophilic and hydrophobic segments, suitable size and high surface hydrophobicity (Jarpa‐Parra et al ., ). Nevertheless, results showed that egg white protein is still superior in terms of air bubble incorporation and retention in the angel food cake batters.…”

Section: Resultsmentioning

confidence: 97%

“…Lentil protein hydrolysates have potential use as antihypertensive effect (Barbana & Boye, ) as they can serve as angiotensin I‐converting enzyme inhibitor (Barbana & Boye, ). Lentil protein also has demonstrated good foaming (Jarpa‐Parra et al ., ) and emulsifying capacity (Joshi et al ., ; Jarpa‐Parra et al ., ). Both functionalities are key during processing and structure formation of baked goods as they contribute to the aeration and stability of the batter (Sahin, ).…”

Section: Introductionmentioning

confidence: 97%

Quality characteristics of angel food cake and muffin using lentil protein as egg/milk replacer

Jarpa‐Parra

Wong

Wismer

et al. 2017

Int J of Food Sci Tech

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Summary Replacement of animal proteins could be interesting for the food industry because it allows long‐term cost savings, among other reasons. Replacing egg/milk protein (50–100 wt%) by lentil protein (LP) was evaluated on angel cake/muffin quality. The replacement did not significantly affect final product volume, neither the muffins nor the angel food cakes. LP did not affect dough formation and contributed to hold crumb structure building an entangled network in both cake products. In addition, angel cakes and muffins containing LP had significantly lower baking loss than the control. Inferior quality for angel cakes and muffins containing LP was observed regarding hardness and chewiness that increased upon storage, compared to the control. For sensory evaluation in angel cakes, appearance of LP formulations showed lower scores than the control, likely due to the change of crumb colour. Other attributes were not significantly impacted by LP presence. For muffins, M‐100‐LPC formulation showed significant differences with the control for most of the attributes, except appearance and flavour. Indeed, consumers preferred muffins with 100% egg/milk protein replacement, which received higher acceptability scores than control. They also appreciated the ‘nutty’ flavour and moisture of angel cake with 50% egg protein replacement. This research suggests that lentil protein can totally or partially substitute egg/milk protein as foam and emulsion stabiliser in cakes, producing products with satisfactory quality.

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“…Additionally, the same research team studied the structural properties of lentil legumin‐like protein in relation to its air–water interfacial behaviours. They found that the FS was closely related to the surface conformation of the protein, which was strongly influenced by the environmental pH (Jarpa‐Parra et al ., ). Lately, they also studied the foaming properties of lentil legumin‐like protein in the presence of different polysaccharides (guar gum, pectin and xanthan gum) and at different pH values.…”

Section: Lentil Protein Functionalitymentioning

confidence: 97%

“…However, Jarpa‐Parra et al . () classified it as 13S, as a result of a rate‐zonal centrifugation study. They also identified three bands of legumin‐like protein with relative molecular weights of 32, 42 and 47 kDa, corresponding to the acidic polypeptide chains and two bands at 18 and 20 kDa corresponding to the basic polypeptide chains, which coincides with Aydemir & Yemenicioğlu () study for a crude lentil protein extract.…”

Section: Lentil Protein Chemistry and Structurementioning

confidence: 99%

Lentil protein: a review of functional properties and food application. An overview of lentil protein functionality

Jarpa‐Parra

2017

Int J of Food Sci Tech

165

108

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Impact of pH on molecular structure and surface properties of lentil legumin-like protein and its application as foam stabilizer

Cited by 139 publications

References 29 publications

Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein

Effects of enzymatic hydrolysis and ultrafiltration on physicochemical and functional properties of faba bean protein

Quality characteristics of angel food cake and muffin using lentil protein as egg/milk replacer

Lentil protein: a review of functional properties and food application. An overview of lentil protein functionality

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