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Related Experiment Video

Updated: May 22, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
11:56

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids

Published on: May 4, 2018

Salt-tolerant endopeptidases from xerophilic Aspergillus sydowii for potential applications in meat processing.

Shinji Takenaka1, Yasuhiro Oribe1, Jun-Ichi Matsumoto2

  • 1Division of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Japan.

Journal of the Science of Food and Agriculture
|May 21, 2026
PubMed
Summary

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Comparative analysis of lipolytic enzymes involved in the surface fermentation of dried katsuobushi by xerophilic molds.

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Improvement of the halotolerance of a Bacillus serine protease by protein surface engineering.

Journal of basic microbiology·2021

Two enzymes from Aspergillus sydowii MA0196, Oryzin MA0196 and Tryp MA0196, were characterized. Oryzin MA0196 shows potential as a meat-tenderizing enzyme, while Tryp MA0196 aids in katsuobushi byproduct valorization.

Area of Science:

  • Enymology
  • Food Science
  • Biotechnology

Background:

  • Dashigara koji, a fermented katsuobushi product, contains bioactive peptides from protein hydrolysis by Aspergillus sydowii MA0196.
  • The specific enzymes responsible for this proteolysis were not previously identified.

Purpose of the Study:

  • To characterize two major endopeptidases from A. sydowii MA0196: a subtilisin-type protease (Oryzin MA0196) and a chymotrypsin-like serine protease (Tryp MA0196).
  • To investigate the biochemical properties and potential applications of these enzymes.

Main Methods:

  • Biochemical analysis of recombinant Oryzin MA0196 and wild-type Tryp MA0196.
  • Enzyme activity assays across various pH, salt, glycerol, and histidine concentrations.
  • Substrate specificity analysis using casein, myofibrillar proteins, type I collagen, and katsuobushi proteins.
Keywords:
Aspergillus sydowiichymotrypsin‐like serine proteasemeat processingsalt‐tolerant endopeptidasesubtilisin‐type serine protease

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Published on: May 25, 2018

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Last Updated: May 22, 2026

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Published on: May 25, 2018

  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to confirm protein hydrolysis.

    • Main Results:

    • Both Oryzin MA0196 and Tryp MA0196 demonstrated broad pH tolerance and stability under high salt conditions (xerotolerance).
    • Tryp MA0196 maintained high activity at 12.5% NaCl; neither enzyme was inhibited by high histidine concentrations.
    • rOryzin MA0196 effectively hydrolyzed casein, myofibrillar proteins, and collagen, while Tryp MA0196 showed broad substrate activity, particularly on modified myosin-derived proteins in katsuobushi.

    Conclusions:

    • Recombinant Oryzin MA0196 shows promise as a meat-tenderizing enzyme due to its activity on myofibrillar and collagen proteins.
    • Tryp MA0196 plays a specific role in katsuobushi protein degradation and has potential for valorizing katsuobushi byproducts.