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

Chymosin-catalyzed peptide synthesis.

C A Abdel Malak1, G I Lavrenova

  • 1Moscow State University Chemistry Department, USSR.

Biomedica Biochimica Acta
|January 1, 1991
PubMed
Summary
This summary is machine-generated.

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

A comparative study of functional properties of calf chymosin and its recombinant forms.

Biochemistry. Biokhimiia·2006
Same author

Isolation of milk-clotting enzyme from transgenic sheep milk and its comparison with calf chymosin.

Biochemistry. Biokhimiia·2001
Same author

Fluorogenic substrates for assay of chymosin.

Biochemistry. Biokhimiia·2000
Same author

[A study of aspartyl proteases using intramolecularly quenched fluorogenic peptide substrates].

Bioorganicheskaia khimiia·2000
Same author

Buffalo (Bos buffali L.) chymosin purification and properties.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology·1996
Same author

[Co-precipitation of pepsin with products from the enzymatic synthesis of peptides as a factor limiting the effectiveness of the enzyme].

Biokhimiia (Moscow, Russia)·1993

Calf chymosin efficiently synthesizes peptides at pH 4-5, particularly when hydrophobic residues form the new bond. This aspartyl proteinase shows promise for creating mid-length peptides.

Area of Science:

  • Biochemistry
  • Enzymology
  • Peptide Chemistry

Background:

  • Chymosin, an aspartyl proteinase, is known for its role in milk coagulation.
  • Understanding chymosin's enzymatic activity beyond its primary function is crucial for exploring its biotechnological applications.

Purpose of the Study:

  • To investigate the potential of calf chymosin as a catalyst for peptide synthesis.
  • To determine the optimal conditions and substrate specificities for chymosin-catalyzed peptide bond formation.

Main Methods:

  • Enzymatic assays using benzyloxycarbonyl tetra- to hexapeptides.
  • Varying pH conditions, with optimal activity observed at pH 4-5.
  • Characterization of synthesized products, including methyl esters and p-nitroanilides.

Related Experiment Videos

Main Results:

  • Calf chymosin effectively catalyzes peptide synthesis, yielding satisfactory amounts of specific peptide derivatives.
  • Optimal enzyme activity was recorded at a pH range of 4-5.
  • The enzyme's efficiency is significantly influenced by the presence of hydrophobic amino acid residues at the new peptide bond and the nature of adjacent residues.

Conclusions:

  • Calf chymosin demonstrates utility as a biocatalyst for the synthesis of mid-length peptides.
  • The enzyme's specificity, particularly its preference for hydrophobic residues, can be leveraged for targeted peptide synthesis.
  • Further research into chymosin's catalytic properties could expand its applications in peptide chemistry and drug development.