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Comparative effects of high isostatic pressure and thermal processing on the inactivation of Rhizomucor miehei protease
Open accessAbstract
This study compared the inactivation of the proteolytic (PA) and milk-clotting (MCA) activities of Rhizomucor miehei protease by high isostatic pressure (HIP) up to 600 MPa/20 min/25 °C and by a thermal process (TP) up to 72.0°C/30 min. Pressures above 300 MPa caused a loss of enzyme activity, MCA being expressively more affected than PA. The inactivation of the protease showed a nonlinear behavior, converging to a two-component system model (stable and labile fractions). The stable fraction represents higher activity for PA and the labile for MCA. The D-values for stable PA (3.35 ± 0.42 min for HIP and 5.58 ± 0.48 min for TP) and labile MCA (0.34 ± 0.04 min for HIP and 0.47 ± 0.04 min for TP) were significantly lower for the HIP processed enzyme, highlighting the effectiveness of the process in inactivating this enzyme. Therefore, the results highlight HIP at 600 MPa as an optional process to inactivate R. miehei protease (without the use of heat), being more effective than the thermal process.
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“Moreover, this fungal protease remains active throughout the shelf life of cheese, even in cheese with heat-treated grains (Leite Júnior et al., 2016).”
From Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review. (2025) · cites this paper as Leite Júnior et al., 2016
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Research works printed but not linked: 14
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Invited review: Milk-clotting enzymes of microbial origin and their role in cheesemaking-A review.
Wiśniewski, P., Małkowska-Kowalczyk, M., Łobacz, A., Zadernowska, A., & Żulewska, J. (2025) · Journal of dairy science · doi:10.3168/jds.2025-26973 · Cited by 10
Metadata
- Authors
- Leite Júnior, B. R. D. C., Tribst, A. A. L., & Cristianini, M.
- Affiliations
- Universidade Estadual de Campinas (UNICAMP) (BR)
- Venue
- LWT
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 65
- Pages
- 1050-1053
- ISSN
- 0023-6438 (ISSN-L)
- OpenAlex
- W1864851264
- Cited by
- 19
- References
- 0
- Citations by year
- 2025: 1 · 2023: 4 · 2022: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 8
- FWCI
- 2.77
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- LWT (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion)
- Americanae (AECID Library) (submittedVersion, cc-by-nc-nd)
- Funders
- Fundação de Amparo à Pesquisa do Estado de São Paulo (2012/13509-6, 2014/17782-4)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Microbial Inactivation Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Keywords
- thermal processing, enzyme inactivation, proteolytic activity, milk-clotting activity, D-value
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