Micelle-mediated extraction of elderberry blossom by whey protein and naturally derived surfactants.

Classical methods of the extraction of active ingredients from the plant material are expensive, complicated and often environmentally unfriendly. The micelle-mediated extraction method (MME) seems to be a good alternative. In this work, extractions of elderberry blossoms (Flos Sambuci) were performed using MME methods. Several popular surfactants and whey protein concentrate (WPC) was applied in the process. The obtained results were compared with those obtained in extraction by means of water. Antioxidant properties of the extracts were analyzed by using two different methods: reaction with di(phenyl)-(2,4,6-trinitrophenyl)iminoazanium (DPPH) reagent and Follin's method. Furthermore, the flavonoid content in the extracts was determined. The results confirmed that the MME method with using whey protein might be an alternative method for obtaining, rich in natural antioxidants, plant extracts.

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Role of carbohydrate conjugation on the emulsification and antioxidant properties of intact and hydrolysed whey protein concentrate

Food Hydrocolloids ◽

10.1016/j.foodhyd.2018.09.030 ◽

2019 ◽

Vol 88 ◽

pp. 170-179 ◽

Cited By ~ 11

Author(s):

Maria Cermeño ◽

Manuel Felix ◽

Alan Connolly ◽

Elaine Brennan ◽

Bernadette Coffey ◽

...

Keyword(s):

Whey Protein ◽

Antioxidant Properties ◽

Whey Protein Concentrate ◽

Protein Concentrate

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Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study

Foods ◽

10.3390/foods9010064 ◽

2020 ◽

Vol 9 (1) ◽

pp. 64

Author(s):

Fatima Abdelhameed Hussein ◽

Shyan Yea Chay ◽

Mohammad Zarei ◽

Shehu Muhammad Auwal ◽

Azizah Abdul Hamid ◽

...

Keyword(s):

Whey Protein ◽

Antioxidant Properties ◽

Radical Scavenging ◽

Ace Inhibition ◽

Whey Protein Concentrate ◽

Protein Concentrate ◽

Converting Enzyme ◽

Optimum Conditions ◽

Angiotensin I ◽

Angiotensin I Converting Enzyme

Whey protein concentrate (WPC) is a unique source of protein with numerous nutritional and functional values due to the high content of branched-chain amino acid. This study was designed to establish the optimum conditions for Alcalase-hydrolysis of WPC to produce protein hydrolysates with dual biofunctionalities of angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities via response surface methodology (RSM). The results showed that the optimum conditions were achieved at temperature = 58.2 °C, E/S ratio = 2.5%, pH = 7.5 and hydrolysis time = 361.8 min in order to obtain the maximum DH (89.2%), ACE-inhibition (98.4%), DPPH• radical scavenging activity (50.1%) and ferrous ion chelation (73.1%). The well-fitted experimental data to predicted data further validates the regression model adequacy. Current study demonstrates the potential of WPC to generate bifunctional hydrolysates with ACE inhibition and antioxidant activity. This finding fosters the use of WPC hydrolysate as a novel, natural ingredient for the development of functional food products.

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