Literature DB >> 1381647

Some biochemical characteristics of a partially purified extracellular keratinase from Trichophyton schoenleinii.

L M Qin1, S Dekio, J Jidoi.   

Abstract

A Trichophyton schoenleinii (T. schoenleinii) strain from tinea favus was cultured in a liquid medium, from which an extracellular keratinase extract was obtained. The keratinase was partially purified with carboxymethyl-cellulose (CMC) column chromatography. Some biochemical characteristics of the keratinase were then examined. Its molecular weight was estimated to be 38,000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature was 50 degrees C, and the optimal pH value was 5.5. The keratinolytic activity was specifically increased by Fe++ and Fe .

Entities:  

Mesh:

Substances:

Year:  1992        PMID: 1381647     DOI: 10.1016/s0934-8840(11)80618-3

Source DB:  PubMed          Journal:  Zentralbl Bakteriol        ISSN: 0934-8840


  3 in total

1.  Similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases.

Authors:  Helena Gradisar; Jozica Friedrich; Igor Krizaj; Roman Jerala
Journal:  Appl Environ Microbiol       Date:  2005-07       Impact factor: 4.792

2.  Partial purification and some biochemical characteristics of exocellular keratinase from Trichophyton mentagrophytes var. erinacei.

Authors:  T M Muhsin; A H Aubaid
Journal:  Mycopathologia       Date:  2001       Impact factor: 2.574

3.  Partial purification and characterization of a 37 kDa extracellular proteinase from Trichophyton vanbreuseghemii.

Authors:  Hossein Moallaei; Farideh Zaini; Gérald Larcher; Bertrand Beucher; Jean-Philippe Bouchara
Journal:  Mycopathologia       Date:  2006-06       Impact factor: 2.574

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.