title: Keratinous waste decomposition and peptide production by keratinase from Geobacillus stearothermophilus AD-11.
abstract: A keratinolytic proteinase was cloned from thermophilic bacterium Geobacillus stearothermophilus AD-11 and was expressed in Escherichia coli BL21(DE3). Recombinant keratinolytic proteinase (RecGEOker) with an estimated molecular weight of 57 kDa was purified and keratinase activity was measured. RecGEOker showed optimal activity at pH 9 and 60 °C. Recombinant keratinolytic proteinase showed the highest substrate specificity toward keratin from wool > collagen > sodium caseinate > gelatin > and BSA in descending order. RecGEOker is applicable for efficient keratin waste biodegradation and can replace conventional non-biological hydrolysis processes. High-value small peptides obtained from enzymatic biodegradation by RecGEOker are suitable for industrial application in white and/or green biotechnology for use as major additives in various products.
authors.affiliation: Department of Microbiology and Biotechnology, Faculty of Natural Sciences, Vilnius University, M. K. Čiurlionio 21/27, LT-03101 Vilnius, Lithuania. Electronic address: audrius.gegeckas@gf.vu.lt.
authors.forename: Audrius
authors.initials: A
authors.lastname: Gegeckas
authors.affiliation: Department of Microbiology and Biotechnology, Faculty of Natural Sciences, Vilnius University, M. K. Čiurlionio 21/27, LT-03101 Vilnius, Lithuania.
authors.forename: Renata
authors.initials: R
authors.lastname: Gudiukaitė
authors.affiliation: Mass Spectrometry Laboratory, Institute of Biochemistry and Biophysics, Polish Academy of Science, Pawinskiego 5a, 02-106 Warsaw, Poland.
authors.forename: Janusz
authors.initials: J
authors.lastname: Debski
authors.affiliation: Department of Microbiology and Biotechnology, Faculty of Natural Sciences, Vilnius University, M. K. Čiurlionio 21/27, LT-03101 Vilnius, Lithuania.
authors.forename: Donaldas
authors.initials: D
authors.lastname: Citavicius
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D019295:Computational Biology; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability / Q000187:drug effects; D004926:Escherichia coli; D005798:Genes, Bacterial; D001411:Geobacillus stearothermophilus / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D007477:Ions; D007633:Keratins / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D012756:Sheep; D012995:Solubility; D012997:Solvents; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity / Q000187:drug effects; D014866:Waste Products
chemical_list: D004791:Enzyme Inhibitors; D007477:Ions; D008670:Metals; D010455:Peptides; D012997:Solvents; D014866:Waste Products; D007633:Keratins; D010447:Peptide Hydrolases; C035855:keratinase
keywords: Bio-active peptide; Geobacillus stearothermophilus AD-11; Keratin biodegradation; Keratinolytic proteinase; White biotechnology