Structural characterization, catalytic, kinetic and thermodynamic properties of Keratinase from Bacillus pumilus FH9

Abdel–Naby, Mohamed A.; El-Refai, Heba A.; Ibrahim, Mohammad H.A.

doi:10.1016/j.ijbiomac.2017.07.118

Cited by 33 publications

(14 citation statements)

References 38 publications

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“…Regarding the biochemical characterization it could be said that, in general, Bacillus`proteases-with keratinolytic activity-showed basic optimum pHs in the range of 8.0-9.0 (i.e., B. subtilis, B. licheniformis ALW1, and B. pumilus FH9) [34][35][36][37]. B. amyloliquefaciens S13 and Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

“…Cai et al [34] purified a keratinase produced by B. subtilis KD-N2, with an optimum temperature of 55°C. Hamiche et al [36] and Abdel-Naby et al [35] studied keratinases from B. amyloliquefaciens S13 and B. pumilus FH9, reporting its optimum temperatures between 50 and 60°C. Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

“…activation and decrease in the unfolding rate are cited as mechanisms of adaptation, mainly on thermophilic and hyperthermophilic proteins [44]. Abdel-Naby et al [35] and Hashem et al [45] reported activation energies of 24 KJ/mol and 25.3 KJ/mol for the proteases with keratinolytic activity from the mesophylls B. pumilus FH9 and B. licheniformis ALW1. Thermal stability of proteolytic extracts of B. cytotoxicus strains was a common feature that it is observed among Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

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The keratinolytic bacteria Bacillus cytotoxicus as a source of novel proteases and feather protein hydrolysates with antioxidant activities

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Bezus

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2021

Journal of Genetic Engineering and Biotechnology

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Background Argentina’s geothermal areas are niches of a rich microbial diversity. In 2020, species of Bacillus cytotoxicus were isolated for the first time from these types of pristine natural areas. Bacillus cytotoxicus strains demonstrated the capability to grow and degrade chicken feathers with the concomitant production of proteases with keratinolytic activity, enzymes that have multitude of industrial applications. The aim of this research was to study the production of the proteolytic enzymes and its characterization. Also, feather protein hydrolysates produced during fermentation were characterized. Results Among the thermotolerant strains isolated from the Domuyo geothermal area (Neuquén province, Argentina), Bacillus cytotoxicus LT-1 and Oll-15 were selected and put through submerged cultures using feather wastes as sole carbon, nitrogen, and energy source in order to obtain proteolytic enzymes and protein hydrolysates. Complete degradation of feathers was achieved after 48 h. Zymograms demonstrated the presence of several proteolytic enzymes with an estimated molecular weight between 50 and > 120 kDa. Optimum pH and temperatures of Bacillus cytotoxicus LT-1 crude extract were 7.0 and 40 °C, meanwhile for Oll-15 were 7.0 and 50 °C. Crude extracts were inhibited by EDTA and 1,10 phenanthroline indicating the presence of metalloproteases. Feather protein hydrolysates showed an interesting antioxidant potential measured through radical-scavenging and Fe3+-reducing activities. Conclusion This work represents an initial approach on the study of the biotechnological potential of proteases produced by Bacillus cytotoxicus. The results demonstrated the importance of continuous search for new biocatalysts with new characteristics and enzymes to be able to cope with the demands in the market.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The keratinolytic bacteria Bacillus cytotoxicus as a source of novel proteases and feather protein hydrolysates with antioxidant activities

Cavello

Bezus

Cavalitto

2021

Journal of Genetic Engineering and Biotechnology

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“…The species include Bacillus subtilis , Bacillus pumilus , Bacillus lichenifomis , and Bacillus cereus ( Zaraî Jaouadi et al, 2015 ; Bhari et al, 2018 ; Gegeckas et al, 2018 ). Some other bacteria are able to degrade feathers with a high efficiency ( Kim et al, 2005 ; Zaraî Jaouadi et al, 2015 ; Abdel-Naby et al, 2017 ; Arokiyaraj et al, 2019 ; Hamiche et al, 2019 ). Keratin-degrading fungi can be isolated from some tissues of human and animals as the produced keratinase might be important for the fungal infection ( Friedrich et al, 1999 ; Bohacz and Korniłłowicz-Kowalska, 2019 ; Zhang et al, 2019 ).…”

Section: Mechanism Of Action For Keratinasementioning

confidence: 99%

Structure, Application, and Biochemistry of Microbial Keratinases

2021

Front. Microbiol.

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Keratinases belong to a class of proteases that are able to degrade keratins into amino acids. Microbial keratinases play important roles in turning keratin-containing wastes into value-added products by participating in the degradation of keratin. Keratin is found in human and animal hard tissues, and its complicated structures make it resistant to degradation by common proteases. Although breaking disulfide bonds are involved in keratin degradation, keratinase is responsible for the cleavage of peptides, making it attractive in pharmaceutical and feather industries. Keratinase can serve as an important tool to convert keratin-rich wastes such as feathers from poultry industry into diverse products applicable to many fields. Despite of some progress made in isolating keratinase-producing microorganisms, structural studies of keratinases, and biochemical characterization of these enzymes, effort is still required to expand the biotechnological application of keratinase in diverse fields by identifying more keratinases, understanding the mechanism of action and constructing more active enzymes through molecular biology and protein engineering. Herein, this review covers structures, applications, biochemistry of microbial keratinases, and strategies to improve its efficiency in keratin degradation.

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“…Designing of efficient and economic bioprocess of enzymes was dependant on the enzyme stability. The thermodynamic study is considered as one of the essential keys to understand the thermal stability of the enzyme and to judge its capability to be used in industrial field [13,14].…”

Section: Introductionmentioning

confidence: 99%

Optimization, characterization and thermodynamic studies on B. licheniformis ALW1 keratinase

et al. 2018

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O PTIMIZATION of B. licheniformis ALW1 keratinase was investigated by using a Plackett -Burman design (PBD) and Central Composite Design (CCD). PBD showed that galactose, inoculum size and corn steep liquor were the most effective variables played a role in improving the enzyme productivity (87.65U/mL). CCD results recorded an increase in enzyme productivity to about1.4-fold compared to the basal medium (99.1 U/mL). The optimum activity for the partial purified enzyme was obtained at pH 8.5 and 70˚C. The activation and deactivation energy were calculated to be 25.37 kJmol -1 and 73.38 kJmol -1 respectively. The half-life time was 1380,690,530, and383 min. at 50˚C,55˚C,60˚C and 65˚C respectively. Also, D values were 4600,2300,1769, 1277min. at the same degree respectively. ∆G° (kJmol -1 ) kept relatively constant between 50-60˚C (191.49 kJmol -1 -193.31 kJmol -1 ) and noticeably increase at 65˚C (212.86 kJmol -1 ). ∆H° (kJmol -1 ) recorded minor decrease by the increase of temperature. Approximately, most of the tested metals ions have stimulation effect in enzyme activity and MgSO 4 .H 2 O was the best (146%). Among all the tested detergents tween 80 retained 97% of original enzyme activity. DMSO increased the enzyme activity by about 11%, while propanol and acetonitrile reduced the enzyme activity to about 14% and 10% respectively. All the reducing agents had a stimulating effect on enzyme activity with variable degrees. The enzyme (980 U) had the ability to hydrolyze 74% of the feather to nutritional valuable protein.

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Structural characterization, catalytic, kinetic and thermodynamic properties of Keratinase from Bacillus pumilus FH9

Cited by 33 publications

References 38 publications

The keratinolytic bacteria Bacillus cytotoxicus as a source of novel proteases and feather protein hydrolysates with antioxidant activities

The keratinolytic bacteria Bacillus cytotoxicus as a source of novel proteases and feather protein hydrolysates with antioxidant activities

Structure, Application, and Biochemistry of Microbial Keratinases

Optimization, characterization and thermodynamic studies on B. licheniformis ALW1 keratinase

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