Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Characterization of byssochlamyopeptidase A.

P S Sun, F S Chu

    Biochimica Et Biophysica Acta
    |May 10, 1979
    PubMed
    Summary

    Byssochlamyopeptidase A, a chymosin-like enzyme, shows specific milk-clotting properties and casein proteolysis. Its activity is inhibited by certain chemicals but is less pH-sensitive than pepsin.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    [The regulatory function of tumor-infiltrating Th9 cells to anti-tumor activity of CD8(+) T cells in patients with gastric cancer].

    Zhonghua zhong liu za zhi [Chinese journal of oncology]·2022
    Same author

    An Indirect Enzyme-Linked Immunosorbent Assay for T-2 Toxin in Biological Fluids.

    Journal of food protection·2019
    Same author

    Enzyme-Linked Immunosorbent Assay of Mycotoxins Using Nylon Bead and Terasaki Plate Solid Phases.

    Journal of food protection·2019
    Same author

    Light-regulated protein and mRNA synthesis in root caps of maize.

    Plant molecular biology·2013
    Same author

    Abscisic acid, xanthoxin and violaxanthin in the caps of gravistimulated maize roots.

    Planta·2013
    Same author

    Yields from blood cultures of patients with suspected paratyphoid fever A.

    Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]·2013

    Area of Science:

    • Enzymology
    • Food Science
    • Biochemistry

    Background:

    • Byssochlamyopeptidase A is a chymosin-like enzyme from Byssochlamys fulva.
    • Understanding its properties is crucial for potential applications in food processing.

    Purpose of the Study:

    • To characterize the enzyme properties of byssochlamyopeptidase A.
    • To investigate its stability, pH sensitivity, and substrate specificity.

    Main Methods:

    • Enzyme purity was confirmed via electrophoresis and immunochemistry.
    • Enzyme activity was tested against various metallic cations and chemical agents.
    • Milk clotting activity and casein fraction proteolysis were analyzed.
    • Substrate specificity was determined using synthetic dipeptides and tripeptides.

    Main Results:

    • The enzyme was electrophoretically and immunochemically pure.
    • Hg2+, N-Bromosuccinimide, and I2 significantly affected enzyme activity.
    • Byssochlamyopeptidase A demonstrated lower pH sensitivity than pepsin for milk clotting.
    • Proteolysis was most extensive on alpha-casein, followed by kappa-casein, and least on beta-casein.
    • The enzyme specifically hydrolyzed Phe-Tyr and Gly-Phe-Phe, but not Ac-Phe-Tyr(I2).

    Conclusions:

    • Byssochlamyopeptidase A possesses distinct enzymatic properties relevant to milk clotting and casein modification.
    • Its stability and specific substrate interactions offer potential for targeted applications.

    Related Experiment Videos