“…5 indicated that the inoculation of the fermentation medium with 5% of 48 h old inoculum produced the highest value of keratinase (72.2 U/ml). This was in agreement with what was reported by other researchers [27], [29], [11].Fig. 5The effect of inoculums size on keratinase production by B. licheniformis ALW1.…”
Section: Resultssupporting
confidence: 93%
“…), actinomycetes ( Streptomyces pactum , S. thermoviolaceus , Thermoactinomyces candidus , etc.) and several bacterial species ( Pseudomonas aeruginosa , Microbacterium sp., Bacillus licheniformis and B. pumilus ) were reported to produce keratinase which is the specific class of proteolytic enzymes cleaving keratin containing substrates [9], [10], [11].…”
Keratinase are proteolytic enzymes which have gained much attention to convert keratinous wastes that cause huge environmental pollution problems. Ten microbial isolates were screened for their keratinase production. The most potent isolate produce 25.2 U/ml under static condition and was primarily identified by partial 16s rRNA gene sequence as Bacillus licheniformis ALW1. Optimization studies for the fermentation conditions increased the keratinase biosynthesis to 72.2 U/ml (2.9-fold). The crude extracellular keratinase was optimally active at pH 8.0 and temperature 65 °C with 0.7% soluble keratin as substrate. The produced B. licheniformis ALW1 keratinase exhibited a good stability over pH range from 7 to 9 and over a temperature range 50–60 °C for almost 90 min. The crude enzyme solution was able to degrade native feather up to 63% in redox free system.
“…5 indicated that the inoculation of the fermentation medium with 5% of 48 h old inoculum produced the highest value of keratinase (72.2 U/ml). This was in agreement with what was reported by other researchers [27], [29], [11].Fig. 5The effect of inoculums size on keratinase production by B. licheniformis ALW1.…”
Section: Resultssupporting
confidence: 93%
“…), actinomycetes ( Streptomyces pactum , S. thermoviolaceus , Thermoactinomyces candidus , etc.) and several bacterial species ( Pseudomonas aeruginosa , Microbacterium sp., Bacillus licheniformis and B. pumilus ) were reported to produce keratinase which is the specific class of proteolytic enzymes cleaving keratin containing substrates [9], [10], [11].…”
Keratinase are proteolytic enzymes which have gained much attention to convert keratinous wastes that cause huge environmental pollution problems. Ten microbial isolates were screened for their keratinase production. The most potent isolate produce 25.2 U/ml under static condition and was primarily identified by partial 16s rRNA gene sequence as Bacillus licheniformis ALW1. Optimization studies for the fermentation conditions increased the keratinase biosynthesis to 72.2 U/ml (2.9-fold). The crude extracellular keratinase was optimally active at pH 8.0 and temperature 65 °C with 0.7% soluble keratin as substrate. The produced B. licheniformis ALW1 keratinase exhibited a good stability over pH range from 7 to 9 and over a temperature range 50–60 °C for almost 90 min. The crude enzyme solution was able to degrade native feather up to 63% in redox free system.
“…The 1–2 % v/v inoculum size was found to be reasonable and lies within the range reported by [ 20 , 21 ] and similar to [ 22 ] findings that reported the use of 2% inoculum size. Inoculum size was not a key player in the keratinase production from B.cereus isolate culture media as increasing or decreasing inoculum size led to a maximum of about ≈6% decline in keratinase production.…”
Highlights
After acclimatization
, Bacillus cereus
isolate produced up to 809 ± 2.49 U/mL of keratinase in 2 days only.
Bacillus cereus
keratinase is stable over wide range of temperatures.
Keratinase decreased the treatment time and increased the treatment efficiency of fucidic acid in skin animal model.
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