Physicochemical characteristics and antigenicity of whey protein hydrolysates obtained with and without pH control

Carvalho, Natália C.; Pessato, Tássia Batista; Fernandes, Luís Gustavo Romani; Zollner, Ricardo de Lima; Netto, Flávia Maria

doi:10.1016/j.idairyj.2017.02.007

Cited by 21 publications

(23 citation statements)

References 44 publications

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“…This decrease in pH during FF hydrolysis is due to the release protons (H + ) during the cleavage of peptide bonds. Similar DH values for WPHs generated under ST and FF conditions have been reported previously by Le Maux et al [12] and Carvalho et al [20]. (http://pepbank.mgh.harvard.edu/) databases for the presence of previously reported bioactive properties.…”

Section: Degree Of Hydrolysis (Dh) Of Wphssupporting

confidence: 88%

“…For instance, the hydrolysates obtained under pH-controlled conditions had higher oxygen radical absorbance capacity (ORAC) values compared to the non pH-controlled hydrolysis reaction. Similar trends were subsequently reported by Carvalho et al [20], where a similar DH but different peptide profiles and surface hydrophobicities were observed following whey protein isolate (WPI) hydrolysis using different hydrolysis conditions.…”

Section: Introductionsupporting

confidence: 86%

“…Butré In addition, these results highlighted that the WPHs generated under different hydrolysis conditions (ST vs. FF) despite having similar DH values (Figure 1), showed different WPC digestion profiles, particularly in the case of DBT-WPHs (Figure 2c,d). Previous studies by Le Maux et al [12], Carvalho et al [20] and Fernández and Kelly [23] also reported different digestion profiles between whey protein hydrolysed under ST and FF conditions (while having comparable DH values). Butré et al [24] demonstrated significant changes in enzyme selectivity (up to 80%) toward cleavage sites in β-lg as a function of pH which also resulted in different hydrolysate molecular mass distribution profiles.…”

Section: Electrophoresis and Molecular Mass Distribution Profilesmentioning

confidence: 86%

“…The antioxidant properties of whey protein hydrolysates as well as whey-derived BAPs have been reported to display numerous functions including free radical scavenging, hydrogen and electron donation, metal ion chelation, quenching of singlet oxygen, peroxide decomposition and inhibition of lipid oxidation [3,9,10,12,[14][15][16][17]19]. It is well documented that the hydrolysis conditions, e.g., temperature, pH and ionic strength and type of salt influence the characteristics of the hydrolysates obtained [12,[20][21][22][23][24][25][26]. The pH of the reaction is considered to be one of the most important parameters during enzymatic hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

“…Changes in pH alter the structure of the enzyme as well as its substrate, and consequently can affect enzyme specificity [22,24]. Enzyme specificity determines the resultant peptide profile [24] and, thus, hydrolysate properties [12,20]. The pH can be controlled throughout an hydrolysis reaction by adding acid or base in order to maintain the enzyme at optimum operating conditions.…”

Section: Introductionmentioning

confidence: 99%

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In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

Kleekayai

Gouic

Deracinois

et al. 2020

Foods

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Bovine whey protein concentrate (WPC) was hydrolysed under pH-stat (ST) and non pH-controlled (free-fall, FF) conditions using Debitrase (DBT) and FlavorPro Whey (FPW). The resultant whey protein hydrolysates (WPHs) were assessed for the impact of hydrolysis conditions on the physicochemical and the in vitro antioxidant and intracellular reactive oxygen species (ROS) generation in oxidatively stressed HepG2 cells. Enzyme and hydrolysis condition dependent differences in the physicochemical properties of the hydrolysates were observed, however, the extent of hydrolysis was similar under ST and FF conditions. Significantly higher (p < 0.05) in vitro and cellular antioxidant activities were observed for the DBT compared to the FPW–WPHs. The WPHs generated under ST conditions displayed significantly higher (p < 0.05) oxygen radical absorbance capacity (ORAC) and Trolox equivalent antioxidant capacity (TEAC) values compared to the FF-WPHs. The impact of hydrolysis conditions was more pronounced in the in vitro compared to the cellular antioxidant assay. WPH peptide profiles (LC-MS/MS) were also enzyme and hydrolysis conditions dependent as illustrated in the case of β-lactoglobulin. Therefore, variation in the profiles of the peptides released may explain the observed differences in the antioxidant activity. Targeted generation of antioxidant hydrolysates needs to consider the hydrolysis conditions and the antioxidant assessment method employed.

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Section: Degree Of Hydrolysis (Dh) Of Wphssupporting

confidence: 88%

Section: Introductionsupporting

confidence: 86%

Section: Electrophoresis and Molecular Mass Distribution Profilesmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

Kleekayai

Gouic

Deracinois

et al. 2020

Foods

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Effects of enzymatic treatments on the hydrolysis and antigenicity reduction of natural cow milk

Liang

Yang

Sun

et al. 2020

Food Science & Nutrition

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Cow milk (CM) allergy is one of the most common food allergies worldwide; the most abundant CM proteins, such as casein (CN), β‐lactoglobulin (β‐LG), and ɑ‐lactalbumin (ɑ‐LA), are all potentially allergenic. Reducing the antigenicity of CM continues to be a major challenge. However, previous studies have focused on the antigenicity of individual allergic CM proteins. Thus, in the present study, we aimed to evaluate the effects of different food‐grade enzymes on the antigenicity of CN, β‐LG, ɑ‐LA in natural CM. The degree of hydrolysis (DH) and molecular mass (MW) distribution of CM hydrolysates were assessed. Additionally, the residual antigenicity of CM hydrolysates was evaluated through enzyme‐linked immunosorbent assay and Western blotting with anti‐CN, anti‐β‐LG, and anti‐ɑ‐LA rabbit polyclonal antibodies. The results showed that Alcalase‐ and Protamex‐mediated hydrolysis could efficiently reduce the antigenicity of CN, β‐LG, and ɑ‐LA, inducing a higher DH, the loss of density of CM proteins, and the increasing levels of low MW (<3 kDa) peptides in CM hydrolysates. Further, Protamex and Alcalase could more efficiently hydrolyze the major allergenic components of CM than the other enzymes, which could represent an advantage for the development of hypoallergenic CM. These findings add further knowledge about the study and development of hypoallergenic CM.

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Enzymatic Production of Bioactive Peptides from Whey Proteins: Their Active Role and Potential Health Benefits

Salvado

Leitão

Fonseca

2020

Enzymes for Solving Humankind's Problems

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Physicochemical characteristics and antigenicity of whey protein hydrolysates obtained with and without pH control

Cited by 21 publications

References 44 publications

In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

Effects of enzymatic treatments on the hydrolysis and antigenicity reduction of natural cow milk

Enzymatic Production of Bioactive Peptides from Whey Proteins: Their Active Role and Potential Health Benefits

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