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1.
Indian J Exp Biol ; 39(7): 650-3, 2001 Jul.
Article in English | MEDLINE | ID: mdl-12019757

ABSTRACT

An heterologous transformation system for entomopathogenic fungi B. bassiana and M. anisopliae was developed based on the use of A. nidulans nitrate reductase gene (niaD). B. bassiana and M. anisopliae niaD stable mutants were selected by treatment of protoplast with ethane methane sulphonate (EMS) and regenerated on chlorate medium. The cloned gene was capable of transforming B. bassiana and M. anisopliae at a frequency of 5.8 to 20 transformants per microg of DNA. Most of them were mitotically stable.


Subject(s)
Hypocreales/enzymology , Hypocreales/genetics , Nitrate Reductases/genetics , Aspergillus niger/enzymology , Aspergillus niger/genetics , Genes, Fungal , Hypocreales/cytology , Mitosis , Mutation , Nitrate Reductase , Transformation, Genetic
2.
Mycopathologia ; 119(3): 161-5, 1992 Sep.
Article in English | MEDLINE | ID: mdl-1435957

ABSTRACT

Two extracellular keratinases of Scopulariopsis brevicaulis were purified and partially characterized. The enzymes were isolated by the techniques of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These keratinases (K I & K II) were purified approximately 33 and 29 fold, respectively. SDS-PAGE of the products of gel filtration chromatography (K I & II) produced only one band each, suggesting homogeneity. The optimum pH for both keratinases was 7.8, while the optimum temperatures were 40 degrees C (K I) and 35 degrees C (K II). Estimated molecular weights were 40-45 KDa and 24-29 KDa for K I & K II respectively. Both keratinases were inhibited by phenylmethylsulfonyl fluoride which suggests a serine residue at or near an active site.


Subject(s)
Mitosporic Fungi/enzymology , Peptide Hydrolases/chemistry , Chromatography, Gel , Electrophoresis, Disc , Enzyme Stability , Molecular Weight , Peptide Hydrolases/isolation & purification
3.
Mycopathologia ; 118(2): 109-14, 1992 May.
Article in English | MEDLINE | ID: mdl-1279428

ABSTRACT

Absidia cylindrospora and Rhizomucor pusillus causal agents of phycomycoses, were cultured on sterile natural keratins in a mineral solution and the keratin degradation products analyzed. The excess of sulphur was removed by oxidation to inorganic sulphate and thiosulphate, which were the main products of sulphitolysis of keratin. The proteolytic activity of the two fungi depended on the nature of the keratin substrate. Human scalp hair was the most favoured keratin substrate by both the fungi.


Subject(s)
Hair/microbiology , Keratins/metabolism , Mucorales/metabolism , Skin/microbiology , Animals , Cattle , Chickens , Dogs , Feathers/microbiology , Hoof and Claw/microbiology , Horns/microbiology , Humans , Hydrogen-Ion Concentration , Sheep , Snakes , Wool/microbiology
4.
Indian J Exp Biol ; 30(2): 103-6, 1992 Feb.
Article in English | MEDLINE | ID: mdl-1381699

ABSTRACT

During hair degradation, majority of organic sulphur was oxidized to inorganic sulphate and thiosulphate by four fungal isolates (Cylindrocarpon lichenicola, Graphium cuneiferum, Microsporum gypseum, and M. fulvum) from gelatin factory soil. Inorganic thiosulphate, an unusual metabolite, was regularly detected in the culture filtrates of all fungi, although in less amounts. Maximum quantity (44 micrograms/ml) was released by G. cuneiferum on 50th day of incubation. All four fungi showed significant extracellular keratinase activity on human hair. Sulphydryl compounds were present in low amounts throughout the experiment. Detection of inorganic sulphate and thiosulphate with significant release of total protein and keratinase and changes in alkalinity, established the role of sulphitolysis and peptidolysis during keratin biodegradation by fungi which ultimately results in complete keratin degradation.


Subject(s)
Fungi/metabolism , Keratins/metabolism , Adult , Female , Gelatin , Hair/metabolism , Humans , Hydrogen-Ion Concentration , In Vitro Techniques , Industry , Peptide Hydrolases/biosynthesis
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