Preprint Article Version 1 This version is not peer-reviewed

From Beer to Cheese: Characterization of Caseinolytic and Milk-Clotting Activities of Proteases Derived from Brewer's Spent Grain (BSG)

Maximiliano Matías Villegas
ORCID logo ,
Johana Nair Silva
,
Florencia Rocío Tito
ORCID logo ,
Claudia Virginia Tonón
,
Fernando Felipe Muñoz
,
Alfonso Pepe
* ,
María Gabriela Guevara
* ORCID logo
Version 1 : Received: 28 October 2024 / Approved: 29 October 2024 / Online: 30 October 2024 (05:18:28 CET)

How to cite: Villegas, M. M.; Silva, J. N.; Tito, F. R.; Tonón, C. V.; Muñoz, F. F.; Pepe, A.; Guevara, M. G. From Beer to Cheese: Characterization of Caseinolytic and Milk-Clotting Activities of Proteases Derived from Brewer's Spent Grain (BSG). Preprints 2024, 2024102242. https://doi.org/10.20944/preprints202410.2242.v1 Villegas, M. M.; Silva, J. N.; Tito, F. R.; Tonón, C. V.; Muñoz, F. F.; Pepe, A.; Guevara, M. G. From Beer to Cheese: Characterization of Caseinolytic and Milk-Clotting Activities of Proteases Derived from Brewer's Spent Grain (BSG). Preprints 2024, 2024102242. https://doi.org/10.20944/preprints202410.2242.v1

Abstract

This study explores the extraction and characterization of proteolytic enzymes from brewer's spent grain (BSG) and their potential as sustainable coagulants in the dairy industry. BSG samples from various beer types (Blonde Ale, IPA, Kölsch, Honey, and Porter) were obtained from two artisanal breweries in Mar del Plata, Argentina. Optimization of caseinolytic activity (CA) and protein extraction was conducted using a Plackett-Burman design, followed by a Box-Behnken design. Optimal protein concentration was achieved at intermediate pH and high temperature, while CA peaked at pH 8.0. The specific caseinolytic activity (SCA) varied among the extracts, with BSG3 showing the highest activity (99.6 U mg⁻¹) and BSG1 the lowest (60.4 U mg⁻¹). Protease inhibitor assays suggested the presence of aspartic, serine, metallo, and cysteine proteases. BSG3 and BSG4 showed the highest hydrolysis rates for α-casein (70% and 78%). For κ-casein, BSG1, BSG2, and BSG3 demonstrated moderate activity (56.5%, 49%, and 55.8), while BSG4 and BSG5 exhibited the lowest activity. Additionally, the milk-clotting activity (MCA) of BSG extracts was comparable to plant-based coagulants like Cynara cardunculus and Ficus carica. These findings highlight the potential of BSG-derived proteases as alternative coagulants for cheese production, offering a sustainable link between the brewing and dairy industries.

Keywords

Circular economy; Barley bioproducts; vegetable rennet; biomass sustainability; food innovation; enzymes

Subject

Biology and Life Sciences, Food Science and Technology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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