ArticleFrontiers in nutrition2021
Heat-Treatments Affect Protease Activities and Peptide Profiles of Ruminants' Milk.
Article in Frontiers in nutrition, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Techniques to Detect and Quantify the Bacterial Metalloprotease AprX in Bovine Milk: A Review.Comprehensive reviews in food science and food safety · 2026Review
- Thermal Versus Ultrasound Inactivation of Bifidobacterium animalis subsp. lactis BB-12: Functional Implications for Postbiotics.Probiotics and antimicrobial proteins · 2026Article
- Multi enzyme production and alginate encapsulation from Bacillus subtilis for stable feed additives.Scientific reports · 2025Article
- Evaluation of UHT milk spoilage caused by proteases from psychrophilic bacteria based on peptidomics.Food chemistry: X · 2024Article
- Peptidomic Analysis of Potential Bioactive Peptides in Mare Milk Under Different Heat Treatment Conditions.Foods (Basel, Switzerland) · 2024Article
- The Impact of Thermal Treatment Intensity on Proteins, Fatty Acids, Macro/Micro-Nutrients, Flavor, and Heating Markers of Milk-A Comprehensive Review.International journal of molecular sciences · 2024Review
- Effect of Heat Treatment on Protein Self-Digestion in Ruminants' Milk.Foods (Basel, Switzerland) · 2023Article
- Article
- Characterization of ACE inhibitory and antioxidant peptides in yak and cow milk hardFood chemistry: X · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases present in milk are heat-sensitive, and their activities increase or decrease depending on the intensity of the thermal treatment applied. The thermal effects on the protease activity are well-known for bovine milk but poorly understood for ovine and caprine milk. This study aimed to determine the non-specific and specific protease activities in casein and whey fractions isolated from raw bovine, ovine, and caprine milk collected in early lactation, and to determine the effects of low-temperature, long-time (63°C for 30 min) and high-temperature, short-time (85°C for 5 min) treatments on protease activities within each milk fraction. The non-specific protease activities in raw and heat-treated milk samples were determined using the substrate azocasein. Plasmin (the main protease in milk) and plasminogen-derived activities were determined using the chromogenic substrate S-2251 (D-Val-Leu-Lys-pNA dihydrochloride). Peptides were characterized using high-resolution liquid chromatography coupled with tandem mass spectrometry. The activity of all native proteases, shown as non-specific proteases, was similar between raw bovine and caprine milk samples, but lower (
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