Study of the Production of Alkaline Keratinases in Submerged Cultures as an Alternative for Solid Waste Treatment Generated in Leather Technology

Six nonpathogenic fungal strains isolated from alkaline soils of Buenos Aires Province, Argentina (Acremonium murorum, Aspergillus sidowii, Cladosporium cladosporoides, Neurospora tetrasperma, Purpureocillium lilacinum (formerly Paecilomyces lilacinus), and Westerdikella dispersa) were tested for th...

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Published inJournal of microbiology and biotechnology Vol. 23; no. 7; pp. 1004 - 1014
Main Authors Cavello, I.A., Research and Development Center for Industrial Fermentations, Argenitina, Chesini, M., Research and Development Center for Industrial Fermentations, Argenitina, Hours, R.A., Research and Development Center for Industrial Fermentations, Argenitina, Cavalitto, S.F., Research and Development Center for Industrial Fermentations, Argenitina
Format Journal Article
LanguageEnglish
Published Seoul Korean Society for Applied Microbiology 01.07.2013
한국미생물·생명공학회
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Summary:Six nonpathogenic fungal strains isolated from alkaline soils of Buenos Aires Province, Argentina (Acremonium murorum, Aspergillus sidowii, Cladosporium cladosporoides, Neurospora tetrasperma, Purpureocillium lilacinum (formerly Paecilomyces lilacinus), and Westerdikella dispersa) were tested for their ability to produce keratinolytic enzymes. Strains were grown on feather meal agar as well as in solid-state and submerged cultures, using a basal mineral medium and “hair waste” as sole sources of carbon and nitrogen. All the tested fungi grew on feather meal agar, but only three of them were capable of hydrolyzing keratin, producing clear zones. Among these strains, P. lilacinum produced the highest proteolytic and keratinolytic activities, both in solid-state and submerged fermentations. The medium composition and culture conditions for the keratinases production by P. lilacinum were optimized. Addition of glucose (5 g/l) and yeast extract (2.23 g/l) to the basal hair medium increased keratinases production. The optimum temperature and initial pH for the enzyme production were 28oC and 6.0, respectively. A beneficial effect was observed when the original concentration of four metal ions, present in the basal mineral medium, was reduced up to 1:10. The maximum yield of the enzyme was 15.96 Uc/ml in the optimal hair medium; this value was about 6.5-fold higher than the yield in the basal hair medium. These results suggest that keratinases from P. lilacinum can be useful for biotechnological purposes such as biodegradation (or bioconversion) of hair waste, leading to a reduction of the environmental pollution caused by leather technology with the concomitant production of proteolytic enzymes and protein hydrolyzates.
Bibliography:A50
G704-000169.2013.23.7.003
ISSN:1017-7825
1738-8872
DOI:10.4014/jmb.1211.11016