Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates

Chabanon, G.; Chevalot, Isabelle; Framboisier, Xavier; Chenu, S.; Marc, Ivan

doi:10.1016/j.procbio.2007.07.009

Cited by 188 publications

(161 citation statements)

References 32 publications

Supporting

Mentioning

134

Contrasting

Order By: Relevance

“…Deteriorated foam stability < 10% was observed at pH 3 throughout all enzymatic settings and at pH 5 after combined enzyme hydrolyses. The increase in foam stability of certain MLPF hydrolysates contrasts with findings of previous studies which reported diminished foam stability of soy protein, rapeseed protein, and cricket protein after enzymatic hydrolysis due to the decomposition of large protein molecules which are needed to enhance viscoelasticity of the air-water interface and stabilize the foam [29,30,33,51].…”

Section: Emulsifying and Foaming Propertiescontrasting

confidence: 98%

“…Different superscripts within one techno-functional parameter and pH level indicate significant differences (p ≤ 0.05; one-way ANOVA, Bonferroni) Samples exhibiting a FS < 10% were not assignable (na) *For two-step hydrolysis (TS 2), the hydrolysis time (t H ) started after 1 h of pre-digestion (see "Combined enzyme treatments") reflects well the extent of protein degradation as shown by DH and SDS-PAGE pattern (see "Protein degradation"). Similar observations of enhanced oil binding properties were reported for globulin-based rapeseed isolate and soy protein isolate after enzymatic hydrolysis [30,51]. The general degree of oil binding found for the hydrolysed and non-hydrolysed MLPF significantly surpasses the OBC of different flours and protein fractions of mealworm and black soldier fly larvae ranging between 0.4 and 0.9 g Oil /g DM [20].…”

Section: Water and Oil Binding Capacitysupporting

confidence: 80%

“…Foam stability between 30-40% at pH 5 and pH 9 was observed for the untreated control while FS was not assignable (na) at pH 3 and pH 7. Initial foam stability of untreated MLPF is considerably low in comparison to conventional food proteins such as soy protein isolate (5% w/v) or rapeseed albumin solution (1.5% w/v) exhibiting an FS of 90% and 76% after 60 and 30 min, respectively [30,51]. Enzymatic hydrolysis resulted in a sharp increase of the foam stability at pH 7 (72%) and a limited improvement at pH 9 (82%).…”

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 99%

“…3. The particular hydrolytic setting and hydrolysis time was chosen for the techno-functional analyses in order to cover the range from low (DH = 7.9) to medium intensive hydrolysis (DH = 15.1) as similarly done by Chabanon et al [30]. Protein solubility of the control ranged from 10 to 22% with its minimum and maximum at pH 5 and pH 9, respectively.…”

Section: Protein Solubilitymentioning

confidence: 99%

“…protein solubility, emulsifying or foaming properties) by limited proteolysis of proteins in comparison to the native, nonhydrolysed protein as already shown for a variety of conventional proteins such as soy proteins [29], rape seed proteins [30] and milk proteins [31]. Similar studies investigating targeted enzymatic hydrolysis of insect proteins to enhance functional properties are scarce.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

Enzymatic hydrolysis of migratory locust (Locusta migratoria L.) protein flour (MLPF) was investigated as a method to improve the techno-functional properties. Experiments were conducted under variation of the applied proteases (Alcalase, Neutrase, Flavourzyme, Papain) or combinations thereof, enzyme-substrate ratio (0.05-1.0% w/w), heat pre-treatment (60-80 °C; 15-60 min), and hydrolysis time (0-24 h). Protein degradation was monitored in terms of degree of hydrolysis (DH) and SDS-PAGE. Solubility, emulsifying, foaming and water/oil binding properties of the hydrolysates were determined. In comparison to the control (DH = 5%), hydrolysis resulted in considerably higher DH values up to 42%. SDS-PAGE profiles revealed a steady decrease of bands between 25 and 75 kDa and an increase of low molecular weight bands (10-15 kDa). However, different heat pre-treatments resulted in impaired hydrolytic cleavage as evidenced by lower DH values. Protein solubility of MLPF hydrolysates was improved over a broad pH range from initially 10-22% up to 55% at alkaline conditions. Furthermore, hydrolysis resulted in enhanced emulsifying activity (54%) at pH 7, improved foamability (326%) at pH 3 and advanced oil binding capacity. The results of this study have clearly demonstrated the potential of targeted enzymatic degradation to improve the techno-functionality of migratory locust protein in order to produce tailored insect-based ingredients for the use in food applications.

show abstract

Section: Emulsifying and Foaming Propertiescontrasting

confidence: 98%

Section: Water and Oil Binding Capacitysupporting

confidence: 80%

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 99%

Section: Protein Solubilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

View full text Add to dashboard Cite

show abstract

Emerging Camelina Protein: Extraction, Modification, and Structural/Functional Characterization

Boyle

Hansen

Hinnenkamp

et al. 2018

J Americ Oil Chem Soc

View full text Add to dashboard Cite

Camelina sativa, a sustainable oilseed crop, is a novel source of plant protein. The aim of this work was to evaluate two protein extraction approaches, alkaline and salt extraction, and determine their impact on the structural and functional properties of camelina protein. Protein yield, content, structural characteristics, and functional properties of the produced camelina protein concentrates (CPC, 70-80% protein) and camelina protein hydrolysates were assessed and compared to reference proteins, whey protein isolate and soy protein isolate (SPI). Compared to alkaline pH extraction, data showed that salt extraction produces less denatured and more functional CPC, composed mainly of cruciferin and napin proteins. The functionality of the salt-extracted CPC was comparable and sometimes better than that of SPI. Specifically, the solubility (~70%) of the salt-extracted CPC at pH 3.4 was significantly (P < 0.05) higher than that (~50%) of SPI. Additionally, salt-extracted CPC had significantly higher emulsification capacity and foaming capacity than SPI. On the other hand, the gelation property of CPC was inferior to that of SPI, an observation attributed to the molecular size of camelina protein compared to soy protein. Upon hydrolysis of CPC with Aspergillus oryzae protease, a limited benefit to solubility was noted at pH 7 postthermal treatment. Overall, results revealed the potential of camelina as a novel source of functional plant protein that might gain a position in the protein market place, and possibly compete with soy protein for several applications targeting the use of plant proteins.a Means in each column with different lowercase letters indicate significant differences among the different extracts according to the Tukey-Kramer multiple means comparison test (P ≤ 0.05). *Significant (P ≤ 0.05) difference between a heated and a nonheated sample.

show abstract

Effect of canola meal fermentation and protein extraction method on the functional properties of resulting protein products

Dai

Stone

et al. 2023

J Americ Oil Chem Soc

View full text Add to dashboard Cite

The present study investigated the effect of solid‐state fermentation (SSF) of cold‐pressed (CP) and hexane‐extracted (HE) canola meals with Aspergillus niger NRRL 334 and Aspergillus oryzae NRRL 5590 on the functionalities of protein products extracted from them. After SSF, proteins were recovered using alkaline extraction‐isoelectric precipitation (AE‐IP) or salt extraction‐dialysis (SE). SSF of the two meal types reduced the protein content of the extracts produced by AE‐IP. There were varied effects to solubility, foaming, and emulsifying properties as a result of SSF under the combined influence of functionality pH, strain, meal type, and protein extraction method. The protein isolate produced from CP meal using SE had increased solubility at pH 7 (from 51.8% to 90.7%) when the meal was fermented with A. oryzae. Both strains resulted in an over twofold increase in the emulsifying activity index (at pH 7) of AE‐IP products from CP meal. For both protein extraction methods, the protein products from A. niger fermented HE meal had better foaming capacity (FC) at pH 7 than the controls (non‐fermented), but reduced FC at pH 3. Overall, regardless of meal fermentation, the SE products were richer in protein and had higher oil holding capacity (OHC), whereas the water holding capacity (WHC) was higher for AE‐IP isolates. SSF of the meals generally improved the O/WHC of the extracted proteins. The findings suggest that canola protein functionality could be effectively modulated by SSF with different microbial strains under various processing conditions to enhance their applicability in the food industry.

show abstract

Hydrolysis of rapeseed protein isolates: Kinetics, characterization and functional properties of hydrolysates

Cited by 188 publications

References 32 publications

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Emerging Camelina Protein: Extraction, Modification, and Structural/Functional Characterization

Effect of canola meal fermentation and protein extraction method on the functional properties of resulting protein products

Contact Info

Product

Resources

About