Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi-pilot scale

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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Evaluation of Nine Semi-pilot Scale Whey Pretreatment Modifications for Producing Whey Protein Concentrate

Journal of Food Science ◽

10.1111/j.1365-2621.1990.tb06798.x ◽

1990 ◽

Vol 55 (2) ◽

pp. 510-515 ◽

Cited By ~ 29

Author(s):

J-C RINN ◽

C.V. MORR ◽

A. SEO ◽

J.G. SURAK

Keyword(s):

Whey Protein ◽

Pilot Scale ◽

Whey Protein Concentrate ◽

Protein Concentrate

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Spray drying of high viscous food concentrates: Investigations on the applicability of an Air-Core-Liquid-Ring (ACLR) nozzle for liquid atomization.

Proceedings of 21th International Drying Symposium ◽

10.4995/ids2018.2018.7289 ◽

2018 ◽

Author(s):

Marc Oliver Wittner ◽

Heike Petra Karbstein ◽

Volker Gaukel

Keyword(s):

Whey Protein ◽

Spray Drying ◽

Particle Morphology ◽

Pilot Scale ◽

Whey Protein Concentrate ◽

Protein Concentrate ◽

Air Core ◽

Liquid Atomization ◽

Pressure Swirl ◽

Liquid Ring

Spray drying is widely used for powder production from liquid concentrates. Often low input temperatures are desired, as many materials, like proteins, are sensitive to heat. However, this demand leads to increased concentrate viscosities. Commonly used pressure swirl atomizers are limited concerning maximum processible viscosity. In this study, a so called Air-Core-Liquid-Ring Atomizer is used for pilot scale spray drying of whey protein concentrate (WPC80) at 40 °C and hence a viscosity of 0.09 Pa s. The produced powder was compared to an industrially produced reference. As a result, no significant differences in particle size distribution and particle morphology were observed. Keywords: spray drying, atomization, ACLR, high viscous feeds, whey protein concentrate.

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Process steps for the preparation of purified fractions of α-lactalbumin and β-lactoglobulin from whey protein concentrates

Journal of Dairy Research ◽

10.1017/s0022029999003519 ◽

1999 ◽

Vol 66 (2) ◽

pp. 225-236 ◽

Cited By ~ 51

Author(s):

GENEVIEVE GÉSAN-GUIZIOU ◽

GEORGES DAUFIN ◽

MARTIN TIMMER ◽

DURITA ALLERSMA ◽

CAROLINE VAN DER HORST

Keyword(s):

Whey Protein ◽

Cheese Whey ◽

Pilot Scale ◽

Whey Protein Concentrate ◽

Protein Concentrate ◽

Whey Protein Concentrates ◽

Sweet Whey ◽

Acid Whey ◽

Gouda Cheese ◽

Β Lactoglobulin

Fractions enriched with α-lactalbumin (α-la) and β-lactoglobulin (β-lg) were produced by a process comprising the following successive steps: clarification–defatting of whey protein concentrate, precipitation of α-lactalbumin, separation of soluble β-lactoglobulin, washing the precipitate, solubilization of the precipitate, concentration and purification of α-la. The present study evaluated the performance of the process, firstly on a laboratory scale with acid whey and then on a pilot scale with Gouda cheese whey. In both cases soluble β-lg was separated from the precipitate using diafiltration or microfiltration and the purities of α-la and β-lg were in the range 52–83 and 85–94% respectively. The purity of the β-lg fraction was higher using acid whey, which does not contain caseinomacropeptide, than using sweet whey. With the pilot scale plant, the recoveries (6% for α-la; 51% for β-lg) were disappointing, but ways of improving each step in the process are discussed.

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