Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Extracellular metalloproteases from bacteria


Bacterial extracellular metalloproteases (BEMPs) are a large group of metal-containing proteases secreted by heterotrophic bacteria. In this review, the diversity, structural characteristics, mechanisms of maturation, physiological roles, and applications of BEMPs are described. BEMPs are distributed among nine families of metalloproteases because of differences in primary sequences and structural characteristics. Until now, all of the BEMPs identified have been endoproteases harboring one catalytic Zn2+ in the active centers. BEMPs are usually synthesized as inactive zymogens with a propeptide that is covalently linked to and inhibits the catalytic domain. The removal of the propeptides of BEMPs is dependent on other proteases or an autocleavage process. The main physiological function of BEMPs is to degrade environmental proteins and peptides for bacterial heterotrophic nutrition. As extracellular proteases, BEMPs vary greatly in enzymology properties to adapt to their respective environments. BEMPs have been widely used in the food and pharmaceutical industries. In order to broaden the application of BEMPs, it is essential to explore novel BEMPs and apply gene/protein engineering to improve the production and properties of promising BEMPs.

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

Fig. 1
Fig. 2


  1. Adekoya OA, Sylte I (2009) The Thermolysin family (M4) of enzymes: therapeutic and biotechnological potential. Chem Biol Drug Des 73:7–16

  2. Ager DJ, Pantaleone DP, Henderson SA, Katrizki AR, Prakash I, Walters DE (1998) Commercial, synthetic nonnutritive sweeteners. Angew Chem Int Ed 37:1802–1817

  3. Ahmed K, Chohan S, Ohashi H, Hirata T, Masaki T, Sakiyama F (2003) Purification, bacteriolytic activity, and specificity of β-lytic protease from Lysobacter sp. IB-9374. J Biosci Bioeng 95:27–34

  4. Arvidson S (1973) Studies on extracellular proteolytic enzymes from Staphylococcus aureus. II. Isolation and characterization of an EDTA-sensitive protease. Biochim Biophys Acta 302:149–157

  5. Ayora S, Götz F (1994) Genetic and biochemical properties of an extracellular neutral metalloprotease from Staphylococcus hyicus subsp. Hyicus. Mol Gen Genet 242:421–430

  6. Barequet IS, Habot-Wilner Z, Mann O, Safrin M, Ohman DE, Kessler E, Rosner M (2009) Evaluation of Pseudomonas aeruginosa staphylolysin (LasA protease) in the treatment of methicillin-resistant Staphylococcus aureus endophthalmitis in a rat model. Graefes Arch Clin Exp Ophthalmol 247:913–917

  7. Barrett AJ (2001) Proteolytic enzymes: nomenclature and classification. In: Beynon R, Bond JS (eds) Proteolytic enzymes. A practical approach, 2nd edn. Oxford University Press, Oxford, pp 1–21

  8. Bélafi-Bakó K (2007) Food manufacture. In: Bhattacharya SK (ed) Enzyme mixtures and complex biosynthesis. Landes Bioscience Press, Texas, pp 29–35

  9. Bond MD, Van Wart HE (1984a) Purification and separation of the individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochem 23:3077–3085

  10. Bond MD, Van Wart HE (1984b) Characterization of individual collagenases from Clostridium histolyticum. Biochem 23:3085–3091

  11. Braun P, de Groot A, Bitter W, Tommassen J (1998) Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J Bacteriol 180:3467–3469

  12. Braun P, Bitter W, Tommassen J (2000) Activation of Pseudomonas aeruginosa elastase in Pseudomonas putida by triggering dissociation of the propepptide-enzyme complex. Microbiol 146:2565–2572

  13. Braun P, Ockhuijsen C, Eppens E, Koster M, Bitter W, Tommassen J (2001) Maturation of Pseudomonas aeruginosa elastase. Formation of the disulfide bonds. J Biol Chem 276:26030–26035

  14. Brint JM, Ohman DE (1995) Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhlR-RhlI, another set of regulators in strain PAOl with homology to the autoinducer-responsive LuxR-LuxI family. J Bacteriol 177:7155–7163

  15. Chang PC, Kuo TC, Tsugita A, Lee YHW (1990) Extracellular metalloprotease gene of Streptomyces cacaoi. J Biol Chem 267:3952–3958

  16. Chen XL, Zhang YZ, Gao PJ, Luan XW (2003) Two different proteases produced by a deep-sea psychrotrophic bacterial strain, Pseudoalteromonas sp. SM9913. Mar Biol 143:989–993

  17. Chen XL, Xie BB, Bian F, Zhao GY, Zhao HL, He HL, Zhou BC, Zhang YZ (2009) Ecological function of myroilysin, a novel bacterial M12 metalloprotease with elastinolytic activity and a synergistic role with collagenase in collagen hydrolysis, in biodegradation of deep-sea high-molecular-weight organic nitrogen. Appl Environ Microbiol 75:1838–1844

  18. Cheung IW, Nakayama S, Hsu MN, Samaranayaka AG, Li-Chan EC (2009) Angiotensin-I converting enzyme inhibitory activity of hydrolysates from oat (Avena sativa) proteins by in silico and in vitro analyses. J Agri Food Chem 57:9234–9242

  19. Clapes P, Torres JL, Adlercreutz P (1995) Enzymatic peptide synthesis in low water content systems: preparative enzymatic synthesis of [Leu]- and [Met]-enkephalin derivatives. Bioorg Med Chem 3:245–255

  20. Clapes P, Pera E, Torres JL (1997) Peptide bond formation by the industrial protease, neutrase, in organic media. Biotechnol Lett 19:1023–1026

  21. Daborn PJ, Waterfield N, Blight MA, Ffrench-Constant RH (2001) Measuring virulence factor expression by the pathogenic bacterium Photorhabdus luminescens in culture and during insect infection. J Bacteriol 183:5834–5839

  22. Dajcs JJ, Hume EB, Moreau JM, Caballero AR, Cannon BM, O’Callaghan RJ (2000) Lysostaphin treatment of methicillin-resistant Staphylococcus aureus keratitis in the rabbit. Invest Ophthalmol Vis Sci 41:1432–1437

  23. Delepelaire P, Wandersman C (1989) Protease secretion by Erwinia chrysanthemi. J Biol Chem 264:9083–9089

  24. Delepelaire P, Wandersman C (1990) Protein secretion in Gram-negative bacteria. J Biol Chem 265:17118–17125

  25. Eijsink VG, Veltman OR, Aukema W, Vriend G, Venema G (1995) Structural determinants of the stability of thermolysin-like proteinases. Nat Struct Biol 2:374–379

  26. Erbeldinger M, Ni X, Halling PJ (1998a) Effect of water and enzyme concentration on thermolysin-catalyzed solid-to-solid peptide synthesis. Biotechnol Bioeng 59:68–72

  27. Erbeldinger M, Ni X, Halling PJ (1998b) Enzymatic synthesis with mainly undissolved substrates at very high concentrations. Enzym Microb Tech 23:141–148

  28. Erbeldinger M, Ni X, Halling PJ (2001) Kinetics of enzymatic solid-to-solid peptide synthesis: synthesis of Z-aspartame and control of acid-base conditions by using inorganic salts. Biotechnol Bioeng 72:69–76

  29. Fernandez M, Ordonez JA, Bruna JM, Herranz B, de la Hoz L (2000) Accelerated ripening of dry fermented sausages. Trends Food Sci Tech 11:201–209

  30. Filloux A, Michel G, Bally M (1998) GSP-dependent protein secretion in Gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa. FEMS Microbiol Rev 22:177–198

  31. Fukushima J, Okuda K (2004) Vibrio collagenase. In: Barrett AJ, Rawlings ND (eds) Handbook of proteolytic enzymes, vol. 1. Elsevier, Amsterdam, pp 414–415

  32. Fukushima J, Takeuchi H, Tanaka E, Hamajima K, Sato Y, Kawamoto S, Morihara K, Keil B, Okuda K (1990) Molecular cloning and partial DNA sequencing of the collagenase gene of Vibrio alginolyticus. Microbiol Immunol 34:977–984

  33. Gao X, Wang J, Yu DQ, Bian F, Xie BB, Chen XL, Zhou BC, Lai LH, Wang ZX, Wu JW, Zhang YZ (2010) Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family. Proc Natl Acad Sci USA 107:17569–17574

  34. Goguen JD, Hoe NP, Subrahmanyam YV (1995) Proteases and bacterial virulence: a view from the trenches. Infect Agents Dis 4:47–54

  35. Grimwood BG, Plummer THJr, Tarentino AL (1994) Purification and characterization of a neutral zinc endopeptidase secreted by Flavobacterium meningosepticum. Arch Biochem Biophys 311:127–132

  36. Gustin JK, Kessler E, Ohman DE (1996) A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion. J Bacteriol 178:6608–6617

  37. Hedtmann A, Fett H, Steffen R, Kramer J (1992) Chemonucleolysis using chymopapain and collagenase. 3-year results of a prospective randomized study. Z Orthop Ihre Grenzgeb 130:36–44

  38. Hirata M, Ishimine T, Hirata A (1997) Development of novel method for enzymatic peptide synthesis utilizing extractive reaction. J Chem Eng Jpn 30:467–477

  39. Iacobucci GA, Brose DJ, Ray RJ, v Eikeren P (1994) Enzymatic membrane method for the synthesis and separation of peptides. US-A 5350681

  40. Inouye K (1992) Effects of salts on thermolysin: Activation of hydrolysis and synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J Biochem 112:335–340

  41. Isowa Y, Ohmori M, Ichikawa T, Mori K, Nonaka Y, Kihara K, Oyama K, Satoh H, Nishimura S (1979) The thermolysin-catalyzed condensation reactions of n-substituted aspartic and glutamic acids with phenylalanine alkyl esters. Tetrahedron Lett 20:2611–2612

  42. Jaspal KK (2008) Lysostaphin: an antistaphylococcal agent. Appl Microbiol Biotechnol 80:555–561

  43. Jin F, Matsushita O, Katayama S, Jin S, Matsushita C, Minami J, Okabe A (1996) Purification, characterization, and primary structure of Clostridium perfringens lambda-toxin, a thermolysin-like metalloprotease. Infect Immun 64:230–237

  44. Karbalaei-Heidari HR, Ziaee A-A, Schaller J, Amoozegar MA (2007) Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004. Enzym Microb Tech 40:266–272

  45. Kessler E, Ohman DE (2004) Pesudolysin. In: Barrett AJ, Rawlings ND (eds) Handbook of proteolytic enzymes, vol 1, 2 edn. Elsevier, Amsterdam, pp 401–409

  46. Kessler E, Safrin M (1988a) Partial purification and characterization of an inactive precursor of Pseudomonas aeruginosa elastase. J Bacteriol 170:1215–1219

  47. Kessler E, Safrin M (1988b) Synthesis, processing, and transport of Pseudomonas aeruginosa elastase. J Bacteriol 170:5241–5247

  48. Kessler E, Safrin M, Olson JC, Ohman DE (1993) Secreted LasA of Pseudomonas aeruginosa is a staphylolytic protease. J Biol Chem 268:7503–7508

  49. Kessler E, Safrin M, Gustin JK, Ohman KE (1998) Elastase and the LasA protease of Pseudomonas aeruginosa are secreted with their propeptides. J Biol Chem 273:30225–30231

  50. Kim HJ, Tamanoue Y, Jeohn GH, Iwamatsu A, Yokota A, Kim YT, Takahashi T, Takahashi K (1997) Purification and characterization of an extracellular metalloprotease from Pseudomonas fluorescens. J Biochem (Tokyo) 212:82–88

  51. Koo HM, VanBrocklin M, McWilliams MJ, Leppla SH, Duesbery NS, Woude GF (2002) Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase. Proc Natl acad Sci USA 99:3052–3057

  52. Kühn D, Dürrschmidt P, Mansfeld J, Ulbrich-Hofmann R (2002) Boilysin and thermolysin in dipeptide synthesis: a comparative study. Biotechnol Appl Biochem 36:71–76

  53. Kumeta H, Hoshino T, Goda T, Okayama T, Shimada T, Ohgiya S, Matsuyama H, Ishizaki K (1999) Identification of a member of the serralysin family isolated from a psychotropic bacterium, Pseudomonas fluorescens 114. Biosci Biotechnol Biochem 63:1165–1170

  54. Kunugi S, Koyasu A, Takahashi S, Oda K (1997) Peptide condensation activity of a neutral protease from Vibrio sp. T1800 (vimelysin). Biotechnol Bioeng 53:387–390

  55. Lee KH, Lee PM, Siaw YS, Morihara K (1992) Aspartame precursor synthesis in water miscible cosolvent catalysed by thermolysin. Biotechnol Lett 14:1159–1164

  56. Leppla SH (2000) Anthrax toxin. In: Aktories K, Just I (eds) Bacterial protein toxins. Springer, Berlin, pp 445–472

  57. Li SL, Norioka S, Sakiyama F (1998) Bacteriolytic activity and specificity of Achromobacter β-lytic protease. J Biochem 124:332–339

  58. Malemud CJ (2006) Matrix metalloproteinases (MMPs) in health and disease: an overview. Front Biosci 11:1696–1701

  59. Malhotra S, Silo-Suh LA, Mathee K, Ohman DE (2000) Proteome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, DsbA. J Bacteriol 182:6999–7006

  60. Mansfeld J (2007) Metalloproteases. In: Polaina J, MacCabe AP (eds) Industrial enzymes. Springer, New York, pp 221–242

  61. Marie-Claire C, Roques BP, Beaumont A (1998) Intramolecular processing of prothermolysin. J Biol Chem 273:5697–5701

  62. Matthews BW, Bp S, Dupourqu D, Jn J, Colman PM (1972) 3-Dimensional structure of thermolysin. Nat New Biol 238:37–41

  63. Matthews BW, Weaver LH, Kester WR (1974) The conformation of thermolysin. J Biol Chem 249:8030–8044

  64. Miyanaga M, Ohmori M, Imamura K, Sakiyama T, Nakanishi K (2000) Kinetics and equilibrium for thermolysin-catalyzed syntheses of dipeptide precursors in aqueous/organic biphasic systems. J Biosci Bioeng 90:43–51

  65. Miyata K, Maejima K, Tomoda K, Isono M (1970) Serratia protease. I. Purification and general properties of the enzyme. Agric Biol Chem 34:310–318

  66. Miyoshi N, Shimizu C, Miyoshi S, Shinoda S (1987) Purification and characterization of Vibrio vulnificus protease. Microbiol Immunol 31:13–25

  67. Monnet V (1995) Oligopeptidases from Lactococcus lactis. Meth Enzymol 248:579–592

  68. Morihara K (1963) Pseudomonas aeruginosa proteinase. I. Purification and general properties. Biochim Biophys Acta 73:113–124

  69. Morihara K (1964) Production of elastase and proteinase by Pseudomonas aeruginosa. J Bacteriol 88:745–757

  70. Morihara K, Tsuzuki H (1977) Production of protease and elastase by Pseudomonas aeruginosa strains isolated from patients. Infect Immun 15:679–685

  71. Murakami Y, Hirata A (1997) Continuous enzymatic synthesis of aspartame precursor at low pH using an extractive reaction. J Ferment Bioeng 84:264–267

  72. Murakami Y, Hirata M, Hirata A (1996) Mathematical approach to thermolysin-catalyzed synthesis of aspartame precursor. J Ferment Bioeng 82:246–252

  73. Murakami Y, Yoshida T, Hirata A (1998) Enzymatic synthesis of N-formyl-L-aspartyl-Lphenylalanine methyl ester (aspartame precursor) utilizing an extractive reaction in aqueous/organic biphasic medium. Biotechnol Lett 20:767–769

  74. Myers LL, Firehammer BD, Shoop DS, Border MM (1984) Bacteroides fragilis: a possible cause of acute diarrheal disease in newborn lambs. Infect Immun 44:241–244

  75. Nakanishi K, Kamikubo T, Matsuno R (1985) Continuous synthesis of N(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester with immobilized thermolysin in an organic solvent. Bio/Technology 3:459–464

  76. Nickerson NN, Joag V, McGavin MJ (2008) Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain. Mol Microbiol 69:1530–1543

  77. Ohta Y, Ogura Y, Wada A (1966) Thermostable protease from thermophilic bacteria. I. Thermostability, physiocochemical properties, and amino acid composition. J Biol Chem 241:5919–5925

  78. Ooshima H, Mori H, Harano Y (1985) Synthesis of aspartame precursor by thermolysin solid in organic solvent. Biotechnol Lett 7:789–792

  79. Patil U, Chaudhari A (2009) Purification and characterization of solvent-tolerant, thermostable, alkaline metalloprotease from alkalophilic Pseudomonas aeruginosa MTCC 7926. J Chem Technol Biotechnol 84:1255–1262

  80. Patron RL, Climo MW, Goldstein BP, Archer GL (1999) Lysostaphin treatment of experimental aortic valve endocarditis caused by a Staphylococcus aureus isolate with reduced susceptibility to vancomycin. Antimicrob Agents Chemother 43:1754–1755

  81. Priest FG (1992) Enzymes extracellular. In: Lederberg J (ed) Encyclopedia of microbiology. Academic, San Diego, pp 451–460

  82. Qian ZJ, Jung WK, Kim SK (2008) Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw. Bioresour Technol 99:1690–1698

  83. Rao MB, Tanksale AM, Ghatge MS, Deshpande VV (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Boil R 62:597–635

  84. Rawlings ND, Barrett AJ (2004) Introduction: metallopeptidases and their clans. In: Barrett AJ, Rawlings ND (eds) Handbook of proteolytic enzymes, vol 1, 2 edn. Elsevier, Amsterdam, pp 231–268

  85. Rawlings ND, Barrett AJ, Bateman A (2010) MEROPS: the peptidase database. Nucleic Acids Res 38:D227–D233

  86. Rival S, Saulner J, Wallach J (2000) On the mechanism of action of pseudolysin: kinetic study of the enzymatic condensation of Z-Ala with Phe-NH2. Biocatal Biotrans 17:417–429

  87. Rohban R, Amoozegar MA, Ventosa A (2009) Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran. J Ind Microbiol Biotechnol 36:333–340

  88. Sánchez-Porro C, Mellado E, Bertoldo C, Antranikian G, Ventosa A (2003) Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76. Extremophiles 7:221–228

  89. Sánchez-Porro C, Mellado E, Pugsley AP, Francetic O, Ventosa A (2009) The haloprotease CPI produced by the moderately halophilic bacterium pseudoalteromonas ruthenica is secreted by the type II secretion pathway. Appl Environ Microbiol 75:4197–4201

  90. Schindler CA, Schuhardt VT (1964) Lysostaphin: a new bacteriolytic agent for the Staphylococcus. Proc Natl Acad Sci USA 51:414–421

  91. Schindler CA, Schuhardt VT (1965) Purification and properties of lysostaphin: a lytic agent for Staphylococcus aureus. Biochim Biophys Acta 97:242–250

  92. Seglen P (1976) Preparation of isolated rat liver cells. Meth Cell Biol 13:29–83

  93. Sharefkin JB, Van Wart HE, Williams SK (1987) Enzymatic harvesting of adult human endothelial cells for use in autogenous endothelial vascular prosthetic seeding. In: Herring MD, Glover JL (eds) Endothelial seeding in vascular surgery. Grune & Stratton, Philadelphia, pp 79–101

  94. Shen S, Chahal B, Majumder K, You SJ, Wu J (2010) Identification of novel antioxidative peptides derived from a thermolytic hydrolysate of ovotransferrin by LC-MS/MS. J Agr Food Chem 58:7664–7672

  95. Shortridge VD, Pato ML, Vasil AI, Vasil ML (1991) Physical mapping of virulence-associated genes in Pseudomonas aeruginosa by transverse alternating-field electrophoresis. Infect Immun 59:3596–3603

  96. Smith H (2002) Discovery of the anthrax toxin: the beginning of studies of virulence determinants regulated in vivo. Int J Med Microbiol 291:411–417

  97. Smith H, Stanley JL (1962) Purification of the third factor of anthrax toxin. J Gen Microbiol 29:517–521

  98. Song L, Li T, Yu R, Yan C, Ren S, Zhao Y (2008) Antioxidant activities of hydrolysates of Arca subcrenata prepared with three proteases. Mar Drugs 6:607–619

  99. Sookkheo B, Sinchaikul S, Phutrakul S, Chen ST (2000) Purification and characterization of the highly thermostable proteases from Bacillus stearothermophilus TLS33. Protein Expr Purif 20:142–151

  100. Takeuchi S, Murase K, Kaidoh T, Maeda T (2000) A metalloprotease is common to swine, avian and bovine isolates of Staphylococcus hyicus. Vet Microbiol 71:169–174

  101. Tan PST, Poolman B, Konings WN (1993) Proteolytic enzymes of Lactococcus lactis. J Dairy Res 60:269–286

  102. Tarentino AL, Quinones G, Grimwood BG, Hauer CR, Plummer TH Jr (1995) Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase. Arch Biochem Biophys 319:281–285

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

  104. Thomas A, Bayat A (2010) The emerging role of Clostridium histolyticum collagenase in the treatment of Dupuytren disease. Therapeut Clin Risk Manag 6:557–572

  105. Titani K, Walsh KA, Ericsson LH, Neurath H, Hermodso M (1972) Amino-acid sequence of thermolysin. Nat New Biol 238:35–37

  106. Toder DS, Gambello MJ, Iglewski BH (1991) Pseudomonas aeruginosa LasA: a second elastase under the transcriptional control of lasR. Mol Microbiol 5:2003–2010

  107. Trine N, Ingolf F, Nes HH (2003) Enterolysin A, a cell wall-degrading bacteriocin from Enterococcus faecalis LMG 2333. Appl Environ Microbiol 69:2975–2984

  108. Tronrud DE, Holden HM, Matthews BW (1987) Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond. Sci 235:571–574

  109. Whitaker DR, Roy C, Tsai CS, Jurasek L (1965) Lytic enzymes of Sorangium sp. Isolation and enzymematic properties of the α- and β-lytic proteases. Can J Biochem 43:1935–1954

  110. Wolters GH, Vos-Scheperkeuter GH, Lin HC, van Schilfgaarde R (1995) Different roles of classIand II Clostridium histolyticum collagenase in rat pancreatic islet isolation. Diabetes 44:227–233

  111. Xie BB, Bian F, Chen XL, He HL, Guo J, Gao X, Zeng YX, Chen B, Zhou BC, Zhang YZ (2009) Cold adaptation of zinc metalloproteases in the thermolysin family from deep-sea and Arctic sea-ice bacteria revealed by catalytic and structural properties and molecular dynamics: New insights into relationship between conformational flexibility and hydrogen-bonding. J Biol Chem 284:9257–9269

  112. Zhou MY, Chen XL, Zhao HL, Dang HY, Luan XW, Zhang XY, He HL, Zhou BC, Zhang YZ (2009) Diversity of both the cultivable protease-producing bacteria and their extracellular proteases in the sediments of the South China Sea. Microbial Ecol 58:582–590

Download references


The work was supported by the National Natural Science Foundation of China (40876072, 31025001, 31070061, and 31000034), the Hi-Tech Research and Development program of China (2006AA09Z414 and SQ2010AA0900521004), the Special Program of China for Marine-scientific Research in the Public Interest (201005032-6), the Natural Science Foundation of Shandong Province, China (JQ200910 and ZR2009DZ002), the Foundation for Young Excellent Scientists in Shandong Province, China (2007BS07007 and BS2010SW015), and Scientific and the Technological Development Program of Shandong Province, China (2010GSF10217).

Author information

Correspondence to Xiu-Lan Chen.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Wu, J., Chen, X. Extracellular metalloproteases from bacteria. Appl Microbiol Biotechnol 92, 253–262 (2011).

Download citation


  • Bacterial extracellular metalloproteases
  • Diversity
  • Structural characteristics
  • Maturation mechanisms
  • Properties
  • Applications