Bacillus subtilis BML5 Isolated from Soil Contaminated with Poultry Waste has Keratinolytic Activity

Imtiaz, Aqsa; Rehman, Abdul

doi:10.17582/journal.pjz/2018.50.1.143.148

Cited by 3 publications

(3 citation statements)

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“…Similarly, pretreatment with 10mM NaOH and sul te improved keratinase activity (95%) by B. cereus and B. subtilis to degrade feather waste [13]. Increase in pH alter cysteine residues to lathionine that makes it accessible for keratinase and alkaline pH was suitable for deamination reaction leading to the release of ammonium ion which increases pH and favor keratinolysis [37]. In this study, pH of the medium increased in shake ask method, similarly enzyme activity was higher (92.5%) at pH 7-10 by Bacillus amyloliquefaciens [42].…”

Section: Discussionmentioning

confidence: 94%

“…The biomass of G. arilaitensis on pretreated feather substituted media revealed that pretreatment enhanced the growth of bacteria. Extreme biomass of B. subtilis and P. aeruginosa was observed at 72 hrs and 5th day [37,38] and biomass of B. licheniformis and the protein content in the medium increased during the process of fermentation [39] which were used as animal feed [2]. Growth of bacteria was determined to access its capacity to use carbon as a sole source from the substrate.…”

Section: Discussionmentioning

confidence: 99%

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Biodegradation of pretreated chicken feather with keratinolytic bacteria Glutamicibacter arilaitensis

Chellapackialakshmi¹,

Ravi²

2022

Preprint

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Purpose Chicken feather is the major waste product of poultry industry that persists in the environment and has become a serious pollutant across the globe. The present study was aimed to check the effect of pretreatment of chicken feather on the keratinolytic potential of chosen bacteria (Glutamicibacter arilaitensis). Methods Chicken feathers were pretreated with 0.1N HCl (strong acid) and 0.1N NaOH (strong base) for 48 hours and then provided as substrate for the bacteria cultured in shake flasks and fermentor. In both categories, parameters such as pH, bacterial growth, bacterial biomass, protein and aminoacid concentration along with protease assay were studied. Further, smears of the two media were prepared and observed microscopically upto 120 hours at 24 hours interval. Antibiotic sensitivity test was performed for bacterial culture. Result The optimum growth and proteolytic activity (24.94 ± 0.19 U/ml) of G. arilaitensis was observed at 72 hours. The concentration of protein (0.49 mg/ml) and amino acid (3.4 mg/ml) was higher in alkali pretreated feather than acidic treatment in both medium. G. arilaitensis was sensitive to antibiotics such as tetracycline, erythromycin, rifampcin, chloramphenicol and streptomycin, however, it was resistant to penicillin and ampicillin. Conclusion It has been found out that, G. arilaitensis was more effective in degrading alkali pretreated feather under fermentation and feather waste can be recycled and converted into valuable products.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Biodegradation of pretreated chicken feather with keratinolytic bacteria Glutamicibacter arilaitensis

Chellapackialakshmi¹,

Ravi²

2022

Preprint

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“…However, not all keratinase production by bacteria was inhibited by glucose. Keratinase production by B. subtilis [33][34] , B. licheniformis 35 and Stenotrophomonas sp. D-1 17 were inhibited by glucose.…”

Section: Effect Of C and N Sources On Keratinase Productionmentioning

confidence: 99%

Keratinase Activity of A Newly Keratinolytic Bacteria, Azotobacter chroococcum B4

Mamangkey¹,

Suryanto²,

Munir³

et al. 2020

J Pure Appl Microbiol

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Keratinase is a proteolytic enzyme capable on degrading the hardy polymeric biomolecule or keratin. In recent days, the utilization of keratinolytic microorganisms is seen as a promising way in recycling the keratin wastes from the avian and mammalians into valuable derived products. Previous study has reported the presence of a keratinolytic bacterium, later identified as Azotobacter chroococcum B4 obtained from dump soils. The present study investigates the enzyme characteristics of keratinase produced by this strain based on the physical appearance of final degraded product using SEM, the molecular weight of keratinase using SDS-PAGE, the effects of nutrition (C/N-source) on strain production of keratinase and the enzyme stability in metal ions solution. The molecular weight of keratinase produced by A. chroococcum B4 was about 30 kDa. Both sucrose and tryptone supplementation increase the keratinase activity by 71.7 and 97.8 U/mL after 96 h of cultivation. Metal ions, Ca 2+ , Mg 2+ , Mn 2+ , Na + , and K + are regarded as activators by increasing the relative activity of keratinase by 117, 166, 111, 113, and 112% respectively, while phenylmethylsulfonyl flouride (PMSF) is regarded as inhibitor by decreasing the relative activity down to 31%. Based on the metal ion characteristics, this strain produced a serine-protease type of keratinase which may further studied for its application in the field.

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Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

et al. 2020

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Keratins are important structural proteins produced by mammals, birds and reptiles. Keratins usually act as a protective barrier or a mechanical support. Millions of tonnes of keratin wastes and low value co-products are generated every year in the poultry, meat processing, leather and wool industries. Keratinases are proteases able to breakdown keratin providing a unique opportunity of hydrolysing keratin materials like mammalian hair, wool and feathers under mild conditions. These mild conditions ameliorate the problem of unwanted amino acid modification that usually occurs with thermochemical alternatives. Keratinase hydrolysis addresses the waste problem by producing valuable peptide mixes. Identifying keratinases is an inherent problem associated with the search for new enzymes due to the challenge of predicting protease substrate specificity. Here, we present a comprehensive review of twenty sequenced peptidases with keratinolytic activity from the serine protease and metalloprotease families. The review compares their biochemical activities and highlights the difficulties associated with the interpretation of these data. Potential applications of keratinases and keratin hydrolysates generated with these enzymes are also discussed. The review concludes with a critical discussion of the need for standardized assays and increased number of sequenced keratinases, which would allow a meaningful comparison of the biochemical traits, phylogeny and keratinase sequences. This deeper understanding would facilitate the search of the vast peptidase family sequence space for novel keratinases with industrial potential.Catalysts 2020, 10, 184 2 of 23 with keratinolytic activity for keratin hydrolysis protects the integrity of the keratin amino acids in most cases and allows control over the peptide size in the hydrolysate that is not readily achievable with other methods [5]. This degree of control allows the production of bespoke medical biomaterials, smart biocomposites, protein feed supplements with enhanced nutritional and bioactive properties as well as personal care products with enhanced functional and bioactive properties.Identifying peptidases with keratinolytic activity is an inherent problem associated with the search for new enzymes. Keratinase activity however appears to be dependent on the accessibility of the keratin substrate to the enzyme [6,7]. Thermochemical or biochemical treatment of the keratin, with emphasis on the reduction of the disulphide bond and disruption of other important bonds involved in the structural stability of keratin like isopeptide, hydrogen and glycolytic bonds [6,[8][9][10], appears to be the prerequisite for enzymatic hydrolysis. Sulphitolysis, which involves reduction of the disulphide bond in keratin, often acts synergistically with keratinases in nature [6,7]. Although destabilization of the keratin structure is a prerequisite for keratin hydrolysis, not all peptidases can hydrolyse keratin. Peptidases like trypsin, papain and pepsin cannot hydrolyse keratin as efficiently ...

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Bacillus subtilis BML5 Isolated from Soil Contaminated with Poultry Waste has Keratinolytic Activity

Cited by 3 publications

References 13 publications

Biodegradation of pretreated chicken feather with keratinolytic bacteria Glutamicibacter arilaitensis

Biodegradation of pretreated chicken feather with keratinolytic bacteria Glutamicibacter arilaitensis

Keratinase Activity of A Newly Keratinolytic Bacteria, Azotobacter chroococcum B4

Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

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