Characterization of a Novel Stenotrophomonas Isolate with High Keratinase Activity and Purification of the Enzyme

Overview

Journal J Ind Microbiol Biotechnol

Publisher Oxford University Press

Specialty Biotechnology

Date 2009 Jan 13

PMID 19137342

Citations 16

Authors

Zhang-Jun Cao

Qi Zhang

Dong-Kai Wei

Li Chen

Jing Wang

Xing-Qun Zhang

Mei-Hua Zhou

Affiliations

Soon will be listed here.

Abstract

A feather-degrading bacterium was isolated from poultry decomposition feathers in China. The strain, named L1, showed significant feather-degrading activity because it grew and reproduced quickly on basal medium containing 10 g/L of native feather as the source of energy, carbon, and nitrogen. According to the phenotypic characteristics and 16S rRNA profile, the isolate belongs to Stenotrophomonas maltophilia. Keratinase activity of the isolate was determined during cultivation on raw feathers at different temperatures and initial pH. Maximum growth and feather-degrading activity of the bacterium were observed at 40 degrees C and initial pH ranging from 7.5 to 8.0. The crude enzyme was purified by ammonium sulphate precipitation, Sephadex G-100 chromatographic and ceramic hydroxyapatite (CHT) chromatographic. Its molecular mass estimated as 35.2 kDa in SDS-PAGE. The enzyme had an optimum activity at the pH was 7.8 and the temperature was 40 degrees C. The keratinase was wholly inhibited by a serine protease inhibitor, PMSF. Its activity was activated or inhibited by different metal ions. The keratinase activity of enzyme from strain L1 functioned on different keratins, such as feather, hair, wool, horn, and so on.

Citing Articles

Identification and characterization of a versatile keratinase, KerZJ, from Stenotrophomonas sp. LMY.

Peng H, Liang M, Zhang J, Liu W, Yang Y, Sun Y World J Microbiol Biotechnol. 2023; 40(1):30.

PMID: 38057391 DOI: 10.1007/s11274-023-03836-5.

Effect of on Tuberculosis.

Li Y, Zhao A, Yu Q, Yu N, Cui Y, Ma X Microbiol Spectr. 2023; 11(4):e0094423.

PMID: 37306591 PMC: 10433947. DOI: 10.1128/spectrum.00944-23.

Valorization of Livestock Keratin Waste: Application in Agricultural Fields.

Chen H, Gao S, Li Y, Xu H, Li W, Wang J Int J Environ Res Public Health. 2022; 19(11).

PMID: 35682267 PMC: 9180014. DOI: 10.3390/ijerph19116681.

Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase From RSA27.

Sharma C, Timorshina S, Osmolovskiy A, Misri J, Singh R Front Microbiol. 2022; 13:882902.

PMID: 35547122 PMC: 9083118. DOI: 10.3389/fmicb.2022.882902.

Isolation of a feather-degrading strain of bacterium from spider gut and the purification and identification of its three key enzymes.

Qu F, Chen Q, Ding Y, Liu Z, Zhao Y, Zhang X Mol Biol Rep. 2018; 45(6):1681-1689.

PMID: 30168098 DOI: 10.1007/s11033-018-4311-8.

References

Langeveld J, Wang J, van de Wiel D, Shih G, Garssen G, Bossers A . Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J Infect Dis. 2003; 188(11):1782-9. DOI: 10.1086/379664. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

Bressollier P, Letourneau F, Urdaci M, Verneuil B . Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus. Appl Environ Microbiol. 1999; 65(6):2570-6. PMC: 91380. DOI: 10.1128/AEM.65.6.2570-2576.1999. View

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

Bockle B, Galunsky B, Muller R . Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530. Appl Environ Microbiol. 1995; 61(10):3705-10. PMC: 167669. DOI: 10.1128/aem.61.10.3705-3710.1995. View

Sangali S, Brandelli A . Isolation and characterization of a novel feather-degrading bacterial strain. Appl Biochem Biotechnol. 2000; 87(1):17-24. DOI: 10.1385/abab:87:1:17. View

Kumar S, Tamura K, Nei M . MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform. 2004; 5(2):150-63. DOI: 10.1093/bib/5.2.150. View

Yamamura S, Morita Y, Hasan Q, Yokoyama K, Tamiya E . Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp. Biochem Biophys Res Commun. 2002; 294(5):1138-43. DOI: 10.1016/S0006-291X(02)00580-6. View

Gupta R, Ramnani P . Microbial keratinases and their prospective applications: an overview. Appl Microbiol Biotechnol. 2006; 70(1):21-33. DOI: 10.1007/s00253-005-0239-8. View

10.

Friedrich A, Antranikian G . Keratin Degradation by Fervidobacterium pennavorans, a Novel Thermophilic Anaerobic Species of the Order Thermotogales. Appl Environ Microbiol. 1996; 62(8):2875-82. PMC: 1388917. DOI: 10.1128/aem.62.8.2875-2882.1996. View

11.

Zaghloul T . Cloned Bacillus subtilis alkaline protease (aprA) gene showing high level of keratinolytic activity. Appl Biochem Biotechnol. 2008; 70-72:199-205. DOI: 10.1007/BF02920136. View

12.

Lucas F, Broennimann O, Febbraro I, Heeb P . High diversity among feather-degrading bacteria from a dry meadow soil. Microb Ecol. 2003; 45(3):282-90. DOI: 10.1007/s00248-002-2032-x. View

13.

Mitsuiki S, Hui Z, Matsumoto D, Sakai M, Moriyama Y, Furukawa K . Degradation of PrP(Sc) by keratinolytic protease from Nocardiopsis sp. TOA-1. Biosci Biotechnol Biochem. 2006; 70(5):1246-8. DOI: 10.1271/bbb.70.1246. View

14.

Yoshioka M, Miwa T, Horii H, Takata M, Yokoyama T, Nishizawa K . Characterization of a proteolytic enzyme derived from a Bacillus strain that effectively degrades prion protein. J Appl Microbiol. 2007; 102(2):509-15. DOI: 10.1111/j.1365-2672.2006.03080.x. View

15.

Riffel A, Brandelli A . Isolation and characterization of a feather-degrading bacterium from the poultry processing industry. J Ind Microbiol Biotechnol. 2002; 29(5):255-8. DOI: 10.1038/sj.jim.7000307. View

16.

Gradisar H, Friedrich J, Krizaj I, Jerala R . Similarities and specificities of fungal keratinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases. Appl Environ Microbiol. 2005; 71(7):3420-6. PMC: 1168971. DOI: 10.1128/AEM.71.7.3420-3426.2005. View

17.

Yamamura S, Morita Y, Hasan Q, Rao S, Murakami Y, Yokoyama K . Characterization of a new keratin-degrading bacterium isolated from deer fur. J Biosci Bioeng. 2005; 93(6):595-600. View

18.

Gradisar H, Kern S, Friedrich J . Keratinase of Doratomyces microsporus. Appl Microbiol Biotechnol. 2000; 53(2):196-200. DOI: 10.1007/s002530050008. View