ArticleIndian journal of pharmaceutical sciences2010
Optimization of cultural conditions for protease production by a fungal species.
Article in Indian journal of pharmaceutical sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Potential of Indonesian Marine Endophytic Fungi as Extracellular Enzymes Producers.Journal of fungi (Basel, Switzerland) · 2026Article
- First report of Fusarium solani species complex infection on mandarin and maltese in Tunisia and semi-quantitative analysis of mycotoxins production in vitro.BMC microbiology · 2026Article
- Vitamin C modulates adrenaline-augmented gastric injury via cardiac troponin/creatine kinase pathway in Wistar rats.Iranian journal of basic medical sciences · 2023Article
- Optimization of a microwave-coupled enzymatic digestion process to prepare peanut peptides.Molecules (Basel, Switzerland) · 2012Article
- Phylogenetic analysis of alkaline proteinase producing fluorescent pseudomonads associated with green gram (Vigna radiata L.) rhizosphere.Folia microbiologica · 2012Article
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Authors and funding
4 authors.
Funding
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Abstract
Studies were carried out on a paddy soil fungal isolate identified to be a strain of Aspergillus niger from Manipal. The parameters that largely impact enzyme production viz., fermentation time, impeller speed, pH, temperature and nutrient supplements were studied. Optimization of production parameters for production of protease was done by the single-parameter mode. Casein served as substrate and proteolytic activity was estimated using Folin-Ciocalteau method at 660 nm. A maximum yield of 71.3 mg tyrosine/g casein substrate was produced in 96 h on a soluble starch medium at pH 4 in shake flask experiments. Production was carried out on a 3-liter fermenter and 40.7 mg of tyrosine was liberated/g of substrate. The enzyme was extracted with 50% ammonium sulfate and sodium dodecyl sulfate-Polyacrylamide gel electrophoresis showed two bands having mw 45.7 kDa and 38.5 kDa, respectively. The enzyme activity was found to be 147.84 U/ml.
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