Wasted-Whey is a principal by-product of the dairy industry which is produced during the manufacture of cheese. Often considered waste for its high polluting power, it contains a wide range of components with some having high nutritional value and biological activities, mainly proteins and bioactive peptides with commercial and nutraceutical potential [1]. Whey proteins, achieved by combining different membrane filtration strategies, are widely used in food, sports nutrition and medical foods. They can be hydrolyzed by employing food grade proteolytic enzymes to obtain whey protein hydrolysates. Protein hydrolysates, a mixture of polypeptides, oligopeptides and amino acids, exhibit numerous bio-functional properties and find use as functional food ingredients with have potential health benefits. This research focused on the recovery and valorization of bioactive peptides from buffalo whey. Using an innovative methodology combining membrane-based fractionation, two different whey, with different protein concentrations, were obtained: concentrated liquid whey (10% protein) and powder whey (76.5% protein). Enzymatic hydrolysis was performed for both types of serum using a food grade enzyme Alcalase®, a serine endopeptidase. Cinetic hydrolysis was conducted for 24 hours with defined temperature. Resulting proteins and peptides were analyzed by advanced mass spectrometry-based proteomics and peptidomics approaches. Results showed that Alcalase activity reduced the α-La and β-Lg protein content during cinetic hydrolysis. Furthermore β-Lg was more sensitive to Alcalase action respect to α -La generating a greatest number of peptides. This study contributes to the understanding valorization and the recovery of bioactive compounds from wasted whey protein, presenting a sustainable approach utilizing dairy by-products.

Recovery and valorization of bioactive peptide from processing waste of the dairy industries

Monica Matuozzo
Primo
;
Andrea Scaloni;Simonetta Caira
2024

Abstract

Wasted-Whey is a principal by-product of the dairy industry which is produced during the manufacture of cheese. Often considered waste for its high polluting power, it contains a wide range of components with some having high nutritional value and biological activities, mainly proteins and bioactive peptides with commercial and nutraceutical potential [1]. Whey proteins, achieved by combining different membrane filtration strategies, are widely used in food, sports nutrition and medical foods. They can be hydrolyzed by employing food grade proteolytic enzymes to obtain whey protein hydrolysates. Protein hydrolysates, a mixture of polypeptides, oligopeptides and amino acids, exhibit numerous bio-functional properties and find use as functional food ingredients with have potential health benefits. This research focused on the recovery and valorization of bioactive peptides from buffalo whey. Using an innovative methodology combining membrane-based fractionation, two different whey, with different protein concentrations, were obtained: concentrated liquid whey (10% protein) and powder whey (76.5% protein). Enzymatic hydrolysis was performed for both types of serum using a food grade enzyme Alcalase®, a serine endopeptidase. Cinetic hydrolysis was conducted for 24 hours with defined temperature. Resulting proteins and peptides were analyzed by advanced mass spectrometry-based proteomics and peptidomics approaches. Results showed that Alcalase activity reduced the α-La and β-Lg protein content during cinetic hydrolysis. Furthermore β-Lg was more sensitive to Alcalase action respect to α -La generating a greatest number of peptides. This study contributes to the understanding valorization and the recovery of bioactive compounds from wasted whey protein, presenting a sustainable approach utilizing dairy by-products.
2024
Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo - ISPAAM
waste whey, food grade enzyme, bioactive compounds
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/547363
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