Cheese Whey Catalytic Conversion for Obtaining a Bioactive Hydrolysate With Reduced Antigenicity

Anna Torkova¹, Kseniya Ryazantzeva², Evgeniya Yu. Agarkova², Mikhail Tsentalovich*¹, Aleksandr Kruchinin² and Tatyana V. Fedorova¹

¹Federal Research Centre “Fundamentals of Biotechnology” of The Russian Academy of Sciences 119071, Russia, Moscow, Leninskiy Prospekt, 33, bld. 2
²Federal State Budgetary Scientific Institution  “All-Russian Research Institute of Dairy Industry” 115093, Russia, Moscow, Lusinovskaya str., 35, bld. 7.

Corresponding Author Email: snowsurfers1@gmail.com

Bioinformatics was used to design a procedure for industrial enzymatic proteolysis of cheese whey. The specificity rules for commercial enzymes were applied to in silico proteolysis of cheese whey proteins. The pattern of antigens was considered, along with molecular descriptors of bitter taste, antioxidant capacity, and anti-hypertensive activity.

The main objective was to obtain hydrolysates with reduced antigenicity and satisfactory sensory properties; an additional goal was to characterize their bioactivity profiles.

Protamex/Alcalase mixtures were first used as multienzyme compositions to obtain non-bitter cheese whey hydrolysates. The multifactor optimization performed for degree of hydrolysis, free amino acid content, and residual antigenicity has revealed the optimal Protamex/Alcalase ratio of 3.5:0.5 and the optimal hydrolysis duration of 90 min.

The hydrolysate obtained using Protamex/Alcalase 3.5:0.5 mixture had a double antioxidant capacity and a 15 times lower ACE-I inhibition concentration IC₅₀ compared to cheese whey concentrate, and an 11 times lower β-LG residual antigenicity.

cheese whey hydrolysis, bioinformatics, debittering, β-lactoglobulin antigenicity. † DH – degree of hydrolysis; FAAC – free amino acid content; RA – residual antigenicity; BT – bitter taste points

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