AI Article Synopsis
- High-resolution ultrasonic spectroscopy (HR-US) was used to detect plasmin activity on β-casein in a controlled buffer solution, focusing on how ultrasonic velocity and attenuation correlate with peptide bond breakdown and β-casein aggregation loss.
- The study demonstrated that HR-US provides a sensitive method for quantifying plasmin levels in milk, showing differences in detection compared to the ELISA method due to varying principles.
- Kinetic analysis of the hydrolysis process indicated a maximum cleavage of 5-6 peptide bonds (2.7% degree of hydrolysis) at a β-casein concentration of 1 mg/mL, with parameters V and K measured during the study.
Article Abstract
High-resolution ultrasonic spectroscopy (HR-US) was applied for precise detection of plasmin activity towards β-casein in buffer at pH 7.8 and 37 °C. The evolution of ultrasonic velocity and ultrasonic attenuation measured at 15.5 MHz is related to the concentration of peptide bonds hydrolyzed and loss of β-casein aggregates, respectively. The ultrasonic assay presents sensitive and direct activity-based quantification of plasmin levels in milk. The variation in plasmin concentration between HR-US and ELISA method owed to the differing detection principles. The real-time ultrasonic profiles of hydrolysis were utilized to describe the kinetic aspect of plasmin activity. The non-linear activity curve was fitted with classic and inverse Michaelis-Menten type models. Within 1-8.6 mg·mL β-casein, the V and K obtained were (6.30 ± 2.21) × 10 mol.kg·min and 10.33 ± 3.50 mg·mL, respectively. The maximum peptide bond cleaved was 5-6 (2.7% degree of hydrolysis) achieved at 1 mg·mL β-casein.
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| http://dx.doi.org/10.1016/j.foodchem.2021.129373 | DOI Listing |
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