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Related Experiment Videos

A non-specific aminopeptidase from Aspergillus.

A M Blinkovsky1, T Byun, K M Brown

  • 1Novo Nordisk Biotech Inc., 1445 Drew Avenue, Davis, CA 95616, USA. alex@nnbt.com

Biochimica Et Biophysica Acta
|July 19, 2000
PubMed
Summary

Researchers identified and characterized aminopeptidase II, a non-specific metalloenzyme from Aspergillus oryzae. This enzyme efficiently hydrolyzes various peptide bonds, with optimal activity at pH 9.5 and 55°C, offering potential applications in biotechnology.

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Area of Science:

  • Enzymology
  • Molecular Biology
  • Biotechnology

Background:

  • Aspergillus oryzae fermentation broth supernatants exhibit aminopeptidase activity.
  • This activity is crucial for releasing amino acids from natural peptides.

Purpose of the Study:

  • To isolate, clone, and characterize a novel aminopeptidase from Aspergillus oryzae.
  • To express the enzyme in heterologous hosts and determine its biochemical properties.

Main Methods:

  • Fractionation of supernatant using anion exchange chromatography.
  • Gene cloning via polymerase chain reaction (PCR) and cDNA library screening.
  • Heterologous expression in Fusarium venenatum and A. oryzae, followed by deglycosylation and SDS-PAGE analysis.

Main Results:

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  • A novel aminopeptidase, named aminopeptidase II, was successfully cloned and expressed.
  • Recombinant aminopeptidase II is a metalloenzyme, approximately 56 kDa after deglycosylation.
  • The enzyme demonstrated broad substrate specificity, with resistance only to X-Pro bonds, and optimal activity at pH 9.5 and 55°C.

Conclusions:

  • Aminopeptidase II is a versatile, non-specific metalloenzyme with potential industrial applications.
  • Its unique substrate specificity and stability make it a valuable tool for peptide hydrolysis.