Production and Characterization of Keratinolytic Proteases Produced by Onygena corvina

Abstract

Poultry farms produce huge quantities of feather waste that causes serious local disposal and accumulative problems and results in environmental pollution. Feathers are composed of β-keratin rich protein and are highly resistant to degradation. The feather degradation potential of the non-pathogenic fungus Onygena corvina was investigated by cultivating this fungus in a medium with duck feathers as the sole carbon and nitrogen source. O. corvina secreted a high level of alkaline protease and keratinase sufficient for degrading duck feathers completely. The optimal conditions for feather keratinolysis were 25ºC, initial pH 8 and feather concentration of 15 g/l. The maximum protease and keratinase activities were found to be 1435 and 72 U/ml, respectively. The protease was active over a broad pH (pH 6-11) and temperature (40-60ºC) range. The keratinase was sensitive to serine protease inhibitors and organic solvents and inhibited by most metal ions, but was stimulated by Ca 2+ and Fe 2+ . Zymogram analysis showed that O. corvina secreted mainly proteases with molecular weight of approximately 35 and 20 kDa. Compared to the fungus Trichoderma asperellum, O. corvina showed higher potential and could be of relevance for bioconverting feather waste into high value products.

Bio-degradation of Feathers Waste by the Staphylococcus epidermidis P3A

“…Feather degradation (%) = (Initial weight of feathers -Final weight of feathers)/Initial weight of feathers×100 25,26 .…”

Optimization of Production and Partial Characterization of Keratinase Produced by Bacillus thuringiensis strain Bt407 Isolated from Poultry Soil

“…which includes Bacillus licheniformis, Bacillus amyloliquefaceins, Brevibacillus brevis US575, Bacillus tequilensis strain Q7, Bacillus pumilus, Bacillus cereus, Bacillus subtilis and Bacillus halodurans (Jaouadi et al, 2013;Jaouadi et al, 2015;Lin et al, 1992;Cortezi et al, 2008;Kumar et al, 2010;Adiguzel et al, 2009;Mazotto et al, 2010;Prakash et al, 2010 (Ionata et al, 2008;Kate and Pethe, 2014;Bakhtiar et al, 2005;Longshaw et al, 2002;Laba et al, 2015 and Fervidobacterium spp. (Allpress et al, 2002;Sangali and Brandelli, 2000, De Toni et al, 2002, Yamamura et al, 2002Shah, 2015;Cao et al, 2009 (Veselá and Friedrich, 2009;Gioppo et al, 2009;Kim, 2007;Patience et al, 2015;Naghy et al, 1998;Friedrich and Kern, 2003;Huang et al, 2015;Duarte et al, 2011).…”

“…AL20 (Bakhtiar et al, 2005), Purpureocillium lilacinum LPS # 876 (Ivana et al,2013), Penicillium spp. Morsy1 (El-Gendy, 2009), Onygena corvina (Huang et al, 2015), Acinetobacter sp. PD 12 (Shah, 2015) (Friedrich and Kern, 2003), Streptomyces flavis 2BG (mesophilic) and Microbispora aerata IMBAS-11A (thermophilic) (Gushterova et al, 2005), Serratia sp.…”

Valorización de residuos sólidos de curtiembre: biotransformación fúngica del pelo vacuno

“…Entre las que pertenecen a hongos no patógenos se encuentran las queratinasas con preferencia en la hidrólisis de aminoácidos aromáticos y no polares en la posición P1 de oligopéptidos sintéticos tales como N-succynil-Ala-Ala-Ala-pNA y N-succynil-Ala-Ala-Pro-Phe-pNA, por ejemplo, pertenecientes al grupo S8 de serin proteasas (Merops;Rawlings et al, 2018). Entre las clasificadas en su mayoría como serin proteasas fueron reportadas las producidas por Doratomyces microsporus y Paecilomyces marquandii , Tritirachium album (proteinasa K) Gunkel et al, 1989), Onygena corvina (Huang, Busk y Lange, 2015), Aspergillus parasiticus (Anitha y Palanivelu, 2013), Aspergillus oryzae , Scopulariopsis brevicaulis , Kocurea rosea , Trichoderma atroviride (Cao, Tan, Liu, Xue y Zhou, 2008). En menor proporción se han caracterizado aquellas pertenecientes a las metaloproteasas producidas, por ejemplo, por Chrysosporium keratinophilum (Dozie, Okeke y Unaeze, 1995).…”