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

[Chymotrypsin-like proteinases in microbial proteolytic complexes].

O S Tsiperovich, M V Kolodzeĭs'ka

    Ukrains'Kyi Biokhimichnyi Zhurnal
    |May 1, 1975
    PubMed
    Summary

    A novel proteinase from Asp. oryzae, termed AO-ct, exhibits potent esterolytic activity, significantly exceeding that of crystalline chymotrypsin. This enzyme displays distinct substrate specificities, offering new insights into proteolytic enzyme function.

    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

    [Oleksandr Solomonovych Tsyperovych--gifted enzymologist, scientist and practician].

    Ukrains'kyi biokhimichnyi zhurnal (1999 )·2008
    Same author

    [Enzymatic activity of chymopsin of various origin].

    Ukrainskii biokhimicheskii zhurnal (1978)·1992
    Same authorSame journal

    [Carboxypeptidases from different microbiolorganisms].

    Ukrains'kyi biokhimichnyi zhurnal·1977
    Same author

    [Effect of deuteration on some IR-spectral characteristics of gelatin].

    Ukrains'kyi biokhimichnyi zhurnal·1977
    Same author

    [Properties of chymotrypsin proteinase from Aspergillus oryzae].

    Ukrains'kyi biokhimichnyi zhurnal·1977
    Same author

    [Gelatin from bone collagen hydrolyzed with Streptomyces griseus protease and its properties].

    Ukrains'kyi biokhimichnyi zhurnal·1975

    Area of Science:

    • Biochemistry
    • Enzymology
    • Microbial Biotechnology

    Background:

    • The proteolytic system of Aspergillus oryzae is a rich source of enzymes with diverse applications.
    • Understanding the specific properties of these enzymes is crucial for optimizing their use in industrial and research settings.

    Purpose of the Study:

    • To characterize a chymotrypsin-type proteinase (AO-ct) from Asp. oryzae, strain "h"-476.
    • To compare the enzymatic properties and substrate specificity of AO-ct with crystalline chymotrypsin.

    Main Methods:

    • Enzyme activity assays using various substrates, including p-nitrophenyl acetate (p-NPA), o-nitro-phenyl acetate, and 2,4-dinitrophenyl acetate (2,4-DNP).
    • Comparative analysis of hydrolysis rates and inhibition patterns with chymotrypsin.
    • Assessment of inhibition by diisopropylfluorophosphate (DFP).

    Main Results:

    • AO-ct demonstrated significantly higher hydrolytic activity on p-NPA (18-20 times) compared to crystalline chymotrypsin.
    • Substrate specificity studies revealed differences in hydrolysis rates influenced by nitrogroup position and number, indicating unique catalytic mechanisms for AO-ct.
    • DFP completely inhibited all tested reactions, confirming the serine protease nature of AO-ct.

    Conclusions:

    • Asp. oryzae produces a potent chymotrypsin-like proteinase (AO-ct) with distinct substrate preferences.
    • AO-ct exhibits superior esterolytic activity on specific substrates compared to chymotrypsin.
    • The findings highlight the potential of microbial proteases like AO-ct in various biotechnological applications.

    Related Experiment Videos