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Related Experiment Videos

A rapid method for measuring protease activity in milk using radiolabeled casein.

G L Christen1

  • 1Department of Animal and Dairy Science, University of Georgia, Athens 30602.

Journal of Dairy Science
|September 1, 1987
PubMed
Summary

A new 30-minute assay using [14C] casein effectively detects protease activity in raw milk, aiding in predicting product shelf life. This radiometric method is highly sensitive and comparable to fluorescein isothiocyanate assays.

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Area of Science:

  • Food Science
  • Biochemistry
  • Analytical Chemistry

Background:

  • Protease activity in raw milk impacts product shelf life.
  • Rapid detection methods are needed for quality control.

Purpose of the Study:

  • To develop and validate a rapid assay for detecting protease activity in raw milk.
  • To compare the performance of a novel radiometric assay with existing methods.

Main Methods:

  • Development of a 30-minute assay using [methyl-14C]-methylated-alpha-casein as a substrate.
  • Comparison with casein fluorescein isothiocyanate, trinitrobenzenesulfonic acid, and Hull procedures.
  • Quantification of protease activity using a Charm analyzer and radiometric detection.

Main Results:

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  • The [14C] casein assay showed linear results with substrate concentration and counting time.
  • Radiometric and fluorescein isothiocyanate assays were equivalent and more sensitive than other methods.
  • The [14C] casein assay was the most sensitive, approximately 10^4 times more than the Hull procedure.

Conclusions:

  • A rapid, sensitive radiometric assay for raw milk protease activity was successfully developed.
  • This assay can aid in predicting the keeping ability of milk products.
  • The [14C] casein method offers a viable alternative for milk quality assessment.