Skip to main content

Advertisement

SpringerLink
Log in

Microbial keratinases and their prospective applications: an overview

  • Mini-Review
  • Published:
Applied Microbiology and Biotechnology Aims and scope Submit manuscript

Abstract

Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide “keratin” recalcitrant to the commonly known proteolytic enzymes trypsin, pepsin and papain. These enzymes are largely produced in the presence of keratinous substrates in the form of hair, feather, wool, nail, horn etc. during their degradation. The complex mechanism of keratinolysis involves cooperative action of sulfitolytic and proteolytic systems. Keratinases are robust enzymes with a wide temperature and pH activity range and are largely serine or metallo proteases. Sequence homologies of keratinases indicate their relatedness to subtilisin family of serine proteases. They stand out among proteases since they attack the keratin residues and hence find application in developing cost-effective feather by-products for feed and fertilizers. Their application can also be extended to detergent and leather industries where they serve as specialty enzymes. Besides, they also find application in wool and silk cleaning; in the leather industry, better dehairing potential of these enzymes has led to the development of greener hair-saving dehairing technology and personal care products. Further, their prospective application in the challenging field of prion degradation would revolutionize the protease world in the near future.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1

Similar content being viewed by others

References

  • Akhtar W, Edwards HGM (1997) Fourier-transform Raman spectroscopy of mammalian and avian keratotic biopolymers. Spectrochim Acta 53:81–90

    Google Scholar 

  • Allpress JD, Mountain G, Gowland PC (2002) Production, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497. Lett Appl Microbiol 34:337–342

    CAS  PubMed  Google Scholar 

  • Anbu P, Gopinath SCB, Hilda A, Lakshmipriya T, Annadurai G (2005) Purification of keratinase from poultry farm isolate Scopulariopsis brevicaulis and statistical optimization of enzyme activity. Enzyme Microb Technol 36:639–647

    CAS  Google Scholar 

  • Apple JK, Boger CB, Brown DC, Maxwell CV, Friesen KG, Roberts WJ, Johnson ZB (2003) Effect of feather meal on live animal performance and carcass quality and composition of growing–finishing swine. J Anim Sci 81:172–181

    CAS  PubMed  Google Scholar 

  • Bernal C, Vidal L, Valdivieso E, Coello N (2003) Keratinolytic activity of Kocuria rosea. World J Microbiol Biotechnol 19:255–261

    CAS  Google Scholar 

  • Betzel C, Dauter Z, Dauter M, Ingelman M, Papendorf G, Wilson KS, Branner S (1988) Crystallization and preliminary X-ray diffraction studies of an alkaline protease from Bacillus lentus. J Mol Biol 204:803–804

    PubMed  Google Scholar 

  • Bockle B, Muller R (1997) Reduction of disulfide bonds by Streptomyces pactum during growth on chicken feathers. Appl Environ Microbiol 63:790–792

    CAS  PubMed  PubMed Central  Google Scholar 

  • Bockle B, Galunsky B, Muller R (1995) Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530. Appl Environ Microbiol 61:3705–3710

    CAS  PubMed  PubMed Central  Google Scholar 

  • Bressollier P, Letourneau F, Urdaci M, Verneuil B (1999) Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus. Appl Environ Microbiol 65:2570–2576

    CAS  PubMed  PubMed Central  Google Scholar 

  • Brutt EH, Ichida JM (1999) Keratinase produced by Bacillus licheniformis. US Patent 5,877,000

  • Cheng SW, Hu HM, Shen SW, Takagi H, Asano M, Tsai YC (1995) Production and characterization of a feather degrading Bacillus licheniformis PWD-1. Biosci Biotechnol Biochem 59:2239–2243

    CAS  PubMed  Google Scholar 

  • Chitte RR, Nalawade VK, Dey S (1999) Keratinolytic activity from the broth of a feather-degrading thermophilic Streptomyces thermoviolaceus strain SD8. Lett Appl Microbiol 28:131–136

    CAS  Google Scholar 

  • Choi JM, Nelson PV (1996) Developing a slow-release nitrogen fertilizer from organic sources. II. Using poultry feathers. J Am Hort Sci 121:634–638

    Google Scholar 

  • De Toni CH, Richter MF, Chagas JR, Henriques JAP, Termignoni C (2002) Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophila strain. Can J Microbiol 48:342–348

    PubMed  Google Scholar 

  • Dozie INS, Okeke CN, Unaeze NC (1994) A thermostable, alkaline-active, keratinolytic proteinase from Chrysosporium keratinophilum. World J Microbiol Biotechnol 10:563–567

    CAS  PubMed  Google Scholar 

  • El-Naghy MA, El-Ktatny MS, Fadl-Allah EM, Nazeer WW (1998) Degradation of chicken feathers by Chrysosporium georgiae. Mycopathologia 143:77–84

    CAS  PubMed  Google Scholar 

  • Evans KL, Crowder J, Miller ES (2000) Subtilisins of Bacillus spp. hydrolyze keratin and allow growth on feathers. Can J Microbiol 46:1004–1011

    CAS  PubMed  Google Scholar 

  • Farag AM, Hassan MA (2004) Purification, characterization and immobilization of a keratinase from Aspergillus oryzae. Enzyme Microb Technol 34:85–93

    CAS  Google Scholar 

  • Friedrich AB, Antranikian G (1996) Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order thermotogales. Appl Environ Microbiol 62:2875–2882

    CAS  PubMed  PubMed Central  Google Scholar 

  • Friedrich J, Kern S (2003) Hydrolysis of native proteins by keratinolytic protease of Doratomyces microsporus. J Mol Catal 21:35–37

    CAS  Google Scholar 

  • Friedrich J, Gradisar H, Mandin D, Chaumont JP (1999) Screening fungi for synthesis of keratinolytic enzymes. Lett Appl Microbiol 28:127–130

    CAS  Google Scholar 

  • Gassessse A, Kaul RH, Gashe BA, Mattiasson B (2003) Novel alkaline proteases from alkalophilic bacteria grown on chicken feather. Enzyme Microb Technol 32:519–524

    Google Scholar 

  • Gousterova A, Braikova D, Goshev I, Christov P, Tishinov K, Tonkova VE, Haertle T, Nedkov P (2005) Degradation of keratin and collagen containing wastes by newly isolated thermoactinomycetes or by alkaline hydrolysis. Lett Appl Microbiol 40:335–340

    CAS  PubMed  Google Scholar 

  • Gunkel FA and Gassen HG (1989) Proteinase K from Tritirachium album Limber: characterization of the chromosomal gene and expression of the cDNA in E. coli. Eur J Biochem 179:185–194

    PubMed  Google Scholar 

  • Gradisar H, Kern S, Friedrich J (2000) Keratinase of Doratomyces microsporus. Appl Microbiol Biotechnol 53:196–200

    CAS  PubMed  Google Scholar 

  • Gregg R (2002). From feathers to degradable plastic. BRI: end of mad cows disease. Triangle Tech Journal (http://www.triangletechjournal.com)

  • Gupta R, Beg QK, Lorenz P (2002) Bacterial alkaline proteases: molecular approaches and industrial applications. Appl Microbiol Biotechnol 59:15–32

    CAS  PubMed  Google Scholar 

  • Hadas A, Kautsky L (1994) Feather meal, a semi-slow-release nitrogen fertilizer for organic farming. Fertil Res 38:165–170

    Google Scholar 

  • Huang Q, Peng Y, Li X (2003) Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilis. Curr Microbiol 43:169–173

    Google Scholar 

  • Ignatova Z, Gousterova A, Spassov G, Nedkov P (1999) Isolation and partial characterization of extracellular keratinase from a wool degrading thermophilic actinomycete strain Thermoactinomyces candidus. Can J Microbiol 45:217–222

    CAS  PubMed  Google Scholar 

  • Ikemura H, Tagaki H, Inouye M (1987) Requirement of pro-sequence for the production of active subtilisin E in Eschericia coli. J Biol Chem 262:7859–7864

    CAS  PubMed  Google Scholar 

  • Jacobs I, Eliasson M, Uhlen M, Flock JI (1985) Cloning, sequencing and expression of subtilisin Carlsberg from Bacillus licheniformis. Nucleic Acids Res 13:8913–8926

    CAS  PubMed  PubMed Central  Google Scholar 

  • Jang JS, Kang DO, Chun MJ, Byun SM (1992) Molecular cloning of Subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis. Biochem Biophys Res Commun 184:277–282

    CAS  PubMed  Google Scholar 

  • Kaul S, Sambali G (1999) Production of extracellular keratinases by keratinophilic fungal species inhabiting feathers of living poultry birds (Gallus domesticus): a comparison. Mycopathologia 146:19–24

    CAS  Google Scholar 

  • Kim JM, Lim WJ, Suh HJ (2001) Feather-degrading Bacillus species from poultry waste. Process Biochem 37:287–291

    CAS  Google Scholar 

  • Kim JS, Kluskens LD, de Vos WM, Huber R, van der Oost J (2004) Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin. J Mol Biol 335:787–797

    CAS  PubMed  Google Scholar 

  • Kluskens LD, Voorhorst WGB, Siezen RJ, Schwerdtfeger RM, Antranikian G, van der Oost J, de Vos WM (2002) Molecular characterization of fervidolysin, a subtilisin-like serine protease from the thermophilic bacterium Fervidobacterium pennivorans. Extremophiles 6:185–194

    CAS  PubMed  Google Scholar 

  • Kreplak L, Doucet J, Dumas P, Briki F (2004) New aspects of the α-helix to β-sheet transition in stretched hard α-keratin fibers. Biophys J 87:640–647

    CAS  PubMed  PubMed Central  Google Scholar 

  • Kurihara M, Markland FS, Smith EL (1972) Subtilisin amylosaccharolyticus. III. Isolation and sequence of the chymotryptic peptides and the complete amino acid sequence. J Biol Chem 247:5617–5631

    CAS  PubMed  Google Scholar 

  • Langeveld JPM, Wang JJ, Van de Wiel DFM, Shih GC, Garssen GJ, Bossers A, Shih JCH (2003) Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J Infect Dis 188:1782–1789

    CAS  PubMed  Google Scholar 

  • Lee GG, Ferket PR, Shih JCH (1991) Improvement of feather digestibility by bacterial keratinase as a feed additive. FASEB J 59:1312

    Google Scholar 

  • Leo WD, van Raamsdonk, Vancutsem J, Zegers J, Frick G, Jorgenson JS, Pinckaers V, Bosch J, Severin IP (2004) The microscopic detection of animal proteins in feeds. Biotechnol Agron Soc Environ 8:241–247

    Google Scholar 

  • Letourneau F, Soussotte V, Bressollier P, Branland P, Verneuil, B (1998) Keratinolytic activity of Streptomyces sp. SK1–02: a new isolated strain. Lett Appl Microbiol 26:77–80

    CAS  PubMed  Google Scholar 

  • Lin X, Lee CG, Casale ES, Shih JCH (1992) Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain. Appl Environ Microbiol 58:3271–3275

    CAS  PubMed  PubMed Central  Google Scholar 

  • Lin X, Kelemen DW, Miller ES, Shih JCH (1995) Nucleotide sequence and expression of ker A, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1. Appl Environ Microbiol 61:1469–1474

    CAS  PubMed  PubMed Central  Google Scholar 

  • Lin X, Shih JCH, Swaisgood HE (1996) Hydrolysis of feather keratin by immobilized keratinase. Appl Environ Microbiol 62:4273–4275

    CAS  PubMed  PubMed Central  Google Scholar 

  • Lin X, Wong SL, Miller ES, Shih JCH (1997) Expression of Bacillus licheniformis PWD-1 keratinase gene in Bacillus subtilis. J Ind Microbiol Biotechnol 19:134–138

    CAS  PubMed  Google Scholar 

  • Lin X, Inglis GD, Yanke LJ, Cheng KJ (1999) Selection and characterization of feather degrading bacteria from conola meal compost. J Ind Microbiol Biotechnol 23:149–153

    CAS  PubMed  Google Scholar 

  • Lucas FS, Broennimann O, Febbraro I, Heeb P (2003) High diversity among feather-degrading bacteria from a dry meadow soil. Microb Ecol 45:282–290

    CAS  PubMed  Google Scholar 

  • Macedo AJ, da Silva WOB, Gava R, Driemeier D, Henriques JAP, Termignoni C (2005) Novel keratinase from Bacillus subtilis S14 exhibiting remarkable dehairing capabilities. Appl Environ Microbiol 71:594–596

    CAS  PubMed  PubMed Central  Google Scholar 

  • Manczinger L, Rozs M, Vagvolgyi Cs, Kevei F (2003) Isolation and characterization of a new keratinolytic Bacillus licheniformis strain. World J Microbiol Biotechnol 19:35–39

    CAS  Google Scholar 

  • Mitsuiki S, Ichikawa M, Oka T, Sakai M, Moriyama Y, Sameshima Y, Goto M, Furukawa K (2004) Molecular characterization of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1. Enzyme Microb Technol 34:482–489

    CAS  Google Scholar 

  • Mohamedin AH (1999) Isolation, identification and some cultural conditions of a protease producing thermophilic Streptomyces strain grown on chicken feathers as a substrate. Int Biodeterior Biodegrad 43:13–21

    CAS  Google Scholar 

  • Mukhopadhyay RP, Chandra AL (1990) Keratinase of a streptomycete. Indian J Exp Biol 28:575–577

    CAS  PubMed  Google Scholar 

  • Musahl C, Aguzzi A (2000) Prions. In: Lederberg J (ed) Encyclopedia of microbiology, 2nd edn. Academic, San Diego, pp 809–823

    Google Scholar 

  • Nakamura T, Yamagata Y, Ichishima E (1992) Peptide synthesis of proteases in organic solvents: medium effect on substrate specificity. Enzyme Microb Technol 14:842–847

    Google Scholar 

  • Nam GW, Lee DW, Lee HS, Lee NJ, Kim BC, Choe EA, Hwang JK, Suhartono MT, Pyun YR (2002) Native feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe. Arch Microbiol 178:538–547

    CAS  PubMed  Google Scholar 

  • Novel JJ, Nickerson W (1959) Decomposition of native keratin by Streptomyces fradiae. J Bacteriol 77:251–263

    Google Scholar 

  • Odetallah NH, Wang JJ, Garlich JD, Shih JCH (2003) Keratinase in starter diets improves growth of broiler chicks. Poultry Sci 82:664–670

    CAS  Google Scholar 

  • Onifade AA, Al-Sane NA, Al-Musallam AA, Al-Zarban S (1998) A review: potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources. Bioresour Technol 66:1–11

    CAS  Google Scholar 

  • Papadopoulos MC (1986) The effect of enzymatic treatment on amino acid content and nitrogen characteristics of feather meal. Anim Feed Sci Technol 16:151–156

    CAS  Google Scholar 

  • Pissuwan D, Suntornsuk W (2001) Production of keratinase by Bacillus sp. FK 28 isolated in Thailand. Kasetsart J 35:171–178

    CAS  Google Scholar 

  • Ramnani P, Gupta R (2004) Optimization of medium composition for keratinase production on feather by Bacillus licheniformis RG1 using statistical methods involving response surface methodology. Biotechnol Appl Biochem 40:491–496

    Google Scholar 

  • Ramnani P, Singh R, Gupta R (2005) Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of feather degradation. Can J Microbiol 51:191–196

    CAS  PubMed  Google Scholar 

  • Riffel A, Lucas F, Heeb P, Brandelli A (2003) Characterization of a new keratinolytic bacterium that completely degrades native feather keratin. Arch Microbiol 179:258–265

    CAS  PubMed  Google Scholar 

  • Rissen S, Antranikian G (2001) Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity. Extremophiles 5:399–408

    Google Scholar 

  • Rozs M, Manczinger L, Vagvolgyi C, Kevei F (2001) Secretion of a trypsin-like thiol protease by a new keratinolytic strain of Bacillus licheniformis. FEMS Microbiol Lett 205:221–224

    CAS  PubMed  Google Scholar 

  • Sangali S, Brandelli A (2000) Feather keratin hydrolysis by a Vibrio sp. strain kr2. J Appl Microbiol 89:735–743

    CAS  PubMed  Google Scholar 

  • Santos RMDB, Firmino AAP, de Sa CM, Felix CR (1996) Keratinolytic activity of Aspergillus fumigatus Fresenius. Curr Microbiol 33:364–370

    CAS  PubMed  Google Scholar 

  • Saravanabhavan S, Aravindhan R, Thanikaivelan P, Rao JR, Nair BU, Ramasami T (2004) A source reduction approach: integrated bio-based tanning methods and the role of enzymes in dehairing and fiber opening. Clean Technol Environ Policy 7:3–14

    Google Scholar 

  • Schrooyen PMM, Radulf B (2004) Keratin-based products and methods for their productions. US Patent 20,040,210,039

  • Schrooyen PMM, Dijkstra PJ, Oberthur RC, Bantjes A, Feijen J (2001) Partially carboxymethylated feather keratins. 2. Thermal and mechanical properties of films. J Agric Food Chem 49:221–230

    CAS  PubMed  Google Scholar 

  • Singh CJ (1999) Exocellular proteases of Malbranchea gypsea and their role in keratin deterioration. Mycopathologia 143:147–150

    CAS  Google Scholar 

  • Sohnle PG, Wagner DK (2000) Fungal infections, cutaneous. In: Lederberg J (ed) Encyclopedia of microbiology, 2nd edn. Academic, San Diego, pp 451–459

    Google Scholar 

  • Stahl ML, Ferrari E (1984) Replacement of the Bacillus subtilis subtilisin structural gene with in-vitro derived mutant. J Bacteriol 158:411–418

    CAS  PubMed  PubMed Central  Google Scholar 

  • Suh HJ, Lee HK (2001) Characterization of a keratinolytic serine protease from Bacillussubtilis KS-1. J Protein Chem 20:165–169

    CAS  PubMed  Google Scholar 

  • Suntornsuk W, Suntornsuk L (2003) Feather degradation by Bacillus sp. FK 46 in submerged cultivation. Bioresour Technol 86:239–243

    CAS  PubMed  Google Scholar 

  • Szabo L, Benedek A, Szabo ML, Barabas G (2000) Feather degradation with a thermotolerant Streptomyces graminofaciens strain. World J Microbiol Biotechnol 16:252–255

    Google Scholar 

  • Takami H, Nogi Y, Horikoshi K (1999) Reidentification of the keratinase-producing facultatively alkaliphilic Bacillus sp. AH-101 as Bacillus halodurans. Extremophiles 3:293–296

    CAS  PubMed  Google Scholar 

  • Thanikaivelan P, Rao JR, Nair BU, Ramasami T (2004) Progress and recent trends in biotechnological methods for leather processing. Trends Biotechnol 22:181–188

    CAS  PubMed  Google Scholar 

  • Thys RCS, Lucas FS, Riffel A, Heeb P, Brandelli A (2004) Characterization of a protease of a feather-degrading Microbacterium species. Lett Appl Microbiol 39:181–186

    CAS  PubMed  Google Scholar 

  • Vidal L, Christen P, Coello MN (2000) Feather degradation by Kocuria rosea in submerged culture. World J Microbiol Biotechnol 16:551–554

    Google Scholar 

  • Vignardet C, Guillaume YC, Michel L, Friedrich J, Millet J (2001) Comparison of two hard keratinous substrates submitted to the action of a keratinase using an experimental design. Int J Pharm 224:115–122

    CAS  PubMed  Google Scholar 

  • Voet D, Voet JG (1995) Three-dimensional structure of proteins. In: Stiefel J (ed) Biochemistry, 2nd edn. Wiley, New York, pp 154–156

    Google Scholar 

  • Wang X, Parsons CM (1997) Effect of processing systems on protein quality of feather meal and hair meals. Poultry Sci 76:491–496

    CAS  Google Scholar 

  • Wang JJ, Shih JCH (1999) Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29. J Ind Microbiol Biotechnol 22:608–616

    CAS  PubMed  Google Scholar 

  • Wang JJ, Swaisgood HE, Shih JCH (2003a) Bioimmobilization of keratinase using Bacillus subtilis and Escherichia coli systems. Biotechnol Bioeng 81:421–429

    CAS  PubMed  Google Scholar 

  • Wang JJ, Swaisgood HE, Shih JCH (2003b) Production and characterization of bio-immobilized keratinase in proteolysis and keratinolysis. Enzyme Microb Technol 32:812–819

    CAS  Google Scholar 

  • Wang JJ, Rojanatavorn K, Shih JCH (2004) Increased production of Bacillus keratinase by chromosomal integration of multiple copies of the kerA gene. Biotechnol Bioeng 87:459–464

    CAS  PubMed  Google Scholar 

  • Wells JA, Ferari E, Henner DJ, Estell DA and Chen EY (1983) Cloning, sequencing and secretion of Bacillus amyloliquefaciens subtilsin in Bacillus subtilis. Nucleic Acids Res 11:7911–7925

    CAS  PubMed  PubMed Central  Google Scholar 

  • Williams CM, Richter CS, Mackenzie JM Jr, Shih JCH (1990) Isolation, identification and characterization of a feather-degrading bacterium. Appl Environ Microbiol 56:1509–1515

    CAS  PubMed  PubMed Central  Google Scholar 

  • Williams CM, Lee CG, Garlich JD, Shih JCH (1991) Evaluation of a bacterial feather fermentation product, feather-lysate as a feed protein. Poultry Sci 70:85–94

    CAS  Google Scholar 

  • Yamamura S, Morita Y, Hasan Q, Rao SR, Murakami Y, Yokoyama K, Tamiya E (2002a) Characterization of a new keratin-degrading bacterium isolated from deer fur. J Biosci Bioeng 93:595–600

    CAS  PubMed  Google Scholar 

  • Yamamura S, Morita Y, Hasan Q, Yokoyama K, Tamiya E (2002b) Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp. Biochem Biophys Res Commun 294:1138–1143

    CAS  PubMed  Google Scholar 

  • Yoshimoto T, Oyama h, Honda T, tone H, Takeshita T, Kamiyama T, Tsuru D (1988) Cloning and expression of subtilisin amylosacchariticus gene. J Biochem 103:1060–1065

    CAS  PubMed  Google Scholar 

  • Zaghloul TI (1998) Cloned Bacillus subtilis alkaline protease (apr A) gene showing high level of keratinolytic activity. Appl Biochem Biotechnol 70–72:199–205

    PubMed  Google Scholar 

  • Zerdani I, Faid M, Malki A (2004) Feather wastes digestion by new isolated strains Bacillus sp. in Morocco. Afr J Biotechnol 3:67–70

    CAS  Google Scholar 

Download references

Acknowledgements

The authors thank the Department of Biotechnology, Government of India, New Delhi, for granting financial assistance through a project on feed enzymes (Sanction no. BT/03/06/2000-PID) and the Council of Scientific and Industrial Research, Government of India, New Delhi, for financial support to P. Ramnani in the form of a Senior Research Fellowship.

Author information

Authors and Affiliations

  1. Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India

    Rani Gupta & Priya Ramnani

Authors
  1. Rani Gupta
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Priya Ramnani
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Rani Gupta.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gupta, R., Ramnani, P. Microbial keratinases and their prospective applications: an overview. Appl Microbiol Biotechnol 70, 21–33 (2006). https://doi.org/10.1007/s00253-005-0239-8

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00253-005-0239-8

Keywords

Search

Navigation