Properties of a new alkaline proteinase from Aspergillus niger.

• BARTHOMEUF Chantal

• POURRAT Henri

• POURRAT Aimee

Abstract

A. niger LCF 9 synthesizes a new aspergillopeptidase of potential interest in therapeutics. The properties and operating range of the enzyme were determined. It is a semi-alkaline aspergillopeptidase (EC 3.4.23.4) with one endopeptidase activity. Its pI is 4.10, its molecular weight is 21000 Da and its A^1%_1cm at 280 nm is 9.75. It rapidly hydrolyzes casein and hemoglobin. Its optimal pH is 7.8 and optimal temperature is 45°C. It is thermally labile above 40°C but can be stabilized by adding calcium ions. It is inhibited by phenylmethylsulfonyl fluoride (PMSF), by ethylenediaminetetraacetic acid (EDTA) and by certain metals ions, e.g. copper, manganese and cobalt ions. It has no dipeptidase or tripeptidase activity and its esterase activity is weak. It has a high collagenase activity and is to our knowledge the only aspergillopeptidase that is active toward benzoyl-arginine p-nitroanilide (BAPNA).

Journal

• Chemical and Pharmaceutical Bulletin

  Chemical and Pharmaceutical Bulletin 37 (5), 1333-1336, 1989

  The Pharmaceutical Society of Japan

Keywords

• serine proteinase
• Aspergillus niger
• molecular weight
• isoelectric point
• property

Details

• CRID: 1390282679142763520
• NII Article ID: 130003944683
• DOI: 10.1248/cpb.37.1333
• ISSN: 13475223
• ISSN: 00092363
• PubMed: 2698284
• Web Site: http://www.jstage.jst.go.jp/article/cpb1958/37/5/37_5_1333/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• Abstract License Flag: Disallowed