Bacterial chitinase: Nature and perspectives for sustainable bioproduction

Bioresources and Bioprocessing

Volumn 2, Issue 1, 2015, Pages

  Yan, Qiang ^a   Fong, Stephen S ^a,b  

^a Virginia Commonwealth University   (United States)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Biopolymer; Bioprocessing; Chitin; Chitinase; Renewable; Sustainability

Indexed keywords

BIOMOLECULES; CELLULOSE; CHITIN; DEGRADATION; INDUSTRIAL CHEMICALS;

BIO-PRODUCTION; BIOPROCESSES; BIOPROCESSING; BUILDING BLOCKES; CHEMICAL MARKETS; CHITIN DEGRADATION; CHITINASES; COMMERCIAL CHEMICALS; MONOMERIC SUGARS; RENEWABLE;

BIOPOLYMERS;

EID: 85020237496     PISSN: None     EISSN: 21974365     Source Type: Journal    
DOI: 10.1186/s40643-015-0057-5     Document Type: Review

References (63)

1. Hasunuma T, Okazaki F, Okai N, Hara KY, Ishii J, Kondo A (2013) A review of enzymes and microbes for lignocellulosic biorefinery and the possibility of their application to consolidated bioprocessing technology. Bioresour Technol 135:513–522
2. Mosier N, Wyman C, Dale B, Elander R, Lee YY, Holtlzapple M, Ladisch M (2005) Features of promising technologies for pretreatment of lignocellulosic biomass. Bioresour Technol 96:673–686
3. Eijsink VGH, Vaaje-Kolstad G, Vårum KM, Horn SJ (2008) Towards new enzymes for biofuels: lessons from chitinase research. Trends Biotechnol 26:228–235
4. Rinaudo M (2006) Chitin and chitosan: properties and applications. Prog in Polym Sci 31:603–632
5. Harti L, Zach S, Seidl-Seiboth V (2012) Fungal chitinase: diversity, mechanistic properties and biotechnological potential. Appl Microbiol and Biotechnol 93:533–543
6. Aam BB, Heggset EB, Norberg AL, Sorlie M, Vårum KM, Eijsink VGH (2010) Production of chitooligosaccharides and their potential applications in medicine. Mar Drugs 8:1482–1517
7. Adrangi S, Faramarzi MA (2013) From bacteria to human: a journal into the world of chitinases. Biotechnol Adv 31:1786–1795
8. Li H, Greene LH (2010) Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding. PLOS one 5(1):e8654–e8664
9. Watanabe T, Kanai R, Kawase T, Tanabe T, Mitsutomi M, Sakuda S, Miyashita K (1999) Family 19 chitinases of Streptomyces species: characterization and distribution. Microbiology 145:3353–3363
10. Watanabe T, Kobori K, Miyashita K, Fujii T, Sakai H, Uchida M, Tanaka H (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J Biol Chem 268:18567–28572
11. Vaaje-Kolstad G, Horn SJ, Sorlie M, Eijsink VGH (2013) The chitinolytic machinery of Serratia marcescens—a model system for enzymatic degradation of recalcitrant polysaccharides. FEBS J 280:3028–3049
12. Hashimoto M, Ikegami T, Seino S, Ohuchi N, Fukada H, Sugiyama J, Shirakawa M, Watanabe T (2002) Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J Bacteriol 182:3045–3054
13. Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773–782
14. Toratani T, Kezuka Y, Nonaka T, Hiragi Y, Watanabe T (2006) Structure of full-length bacterial chitinase containing two fibronectin type III domains revealed by small angle X-ray scattering. Biochem Biophys Res Commun 348:814–818
15. Watanabe T, Ariga Y, Sato U, Toratami T, Hashimoto M, Nikaidou N, Kezuka Y, Nonaka T, Sugiyama J (2002) Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin. Biochem J 376:37–244
16. Watanabe T, Ishibashi A, Ariga Y, Hashimoto M, Nikaidou N, Sugiyama J, Matsumoto T, Nonaka T (2001) Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline-chitin hydrolysis by Bacillus circulans chitinase A1. FEBS Lett 494:74–78
17. Watanabe T, Ariga Y, Sato U, Toratani T, Hashimoto M, Nikaidou N, Kezuka Y, Nonaka T, Sugiyama J (2003) Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin. Biochem J 376:237–244
18. Watanabe T, Suzuki K, Oyanagi W, Ohnishi K, Tanaka H (1990) Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J Biol Chem 265:15659–15665
19. Jee JG, Ikegami T, Hashimoto M, Kawabata T, Ikeguchi M, Watanabe T, Shirakawa M (2002) Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 chitinase A1. J Biol Chem 277:1388–1397
20. Watanabe T, Ito Y, Yamada T, Hashimoto M, Sekine S, Tanaka H (1994) The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J Bacteriol 176:4465–4472
21. Uchiyam T, Katouno F, Nikaidou N, Nonaka T, Sugiyama J, Watanabe T (2001) Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J Biol Chem 276:41343–41349
22. Horn SJ, Sikorski P, Cederkvist JB, Vaaje-Kolstad G, Sørlie M, Synstad B, Vriend G, Vårum KM, Eijsink VGH (2006) Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc Natl Acad Sci USA 103:18089–18094
23. Akira O (1998) Viscosimetric assay for chitinase. In: Willis A, Wood STK (eds) Methods in enzymology. Academic Press, New York
24. Boller T (1998) Colorimetric assay for chitinase. In: Willis A, Wood STK (eds) Methods in enzymology. Academic Press, New York
25. Enrico C (1998) Assay for chitinase using tritiated chitin. In: Willis A, Wood STK (eds) Methods in enzymology. Academic Press, New York
26. Howard MB, Ekborg NA, Weiner RM, Hutcheson SW (2003) Detection and characterization of chitinases and other chitin-modifying enzymes. J Ind Microbiol Biotechnol 30:627–635
27. Zhang PYH, Himmel ME, Mielenz JR (2006) Outlook for cellulose improvement: screening and selection strategies. Biotechnol Adv 24:452–481
28. Eveleigh DE, Mandels M, Andreotti R, Roche C (2009) Measurement of saccharifying cellulose. Biotechnol Biofuels 2:21–28
29. Ferrari AR, Gaber Y, Fraaije MW (2014) A fast, sensitive and easy colorimetric assay for chitinase and cellulose activity detection. Biotechnol Biofuels 7:37–44
30. Shen CR, Chen YS, Yang CJ, Chen JK, Liu CL (2010) Colloid chitin azure is a dispersible, low-cost substrate for chitinase measurements in a sensitive, fast, reproducible assay. Biomol Screening 15:213–217
31. Horri SJ, Eijsink VGH (2004) A reliable reducing end assay for chitooligosaccharides. Carbohydr Polym 56:35–39
32. Price NPJ, Naumann TA (2011) A high-throughput matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry-based assay of chitinase activity. Anal Biochem 411:94–99
33. Thadathil N, Velappan SP (2014) Recent developments in chitosanase research and its biotechnological applications: a review. Food Chem 150:392–399
34. Toratani T, Shoji T, Ikehara T, Suzuki K, Watanabe T (2008) The importance of chitobiase and N-acetylglucosamine (GlcNAc) uptake in N,N ′-diacetylchitobiose [(GlcNAc)2] utilization by Serratia marcescens 2170. Microbiol 154:1326–1332
35. Suginta W, Chenark D, Mizuhara M, Fukamizo T (2010) Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification. BMC Biochem 11:40–51
36. da Silva AF, García-Fraga B, López-Seijas J, Sieiro C (2014) Characterization and optimization of heterologous expression in Escherichia coli of the chitinase encoded by the chiA gene of Bacillus halodurans C-125. Process Biochem 49:1622–1629
37. Songsiriritthigul C, Lapboonrueng S, Pechsrichuang P, Pesatcha P, Yamabhai M (2010) Expression and characterization of Bacillus licheniformis chitinase (ChiA), suitable for bioconversion of chitin waste. Bioresour Technol 101:4096–4103
38. Lobo MDP, Silva FDA, Landim PGC, Cruz PR, de Brito TL, de Medeiros SC, Oliveira JTA, Vasconcelos IM, Pereira HDM, Grangeiro TB (2013) Expression and efficient secretion of a functional chitinase from Chromobacterium violaceum in Escherichia coli. BMC Biotechnol 13:46–60
39. Ghasemi S, Ahmadian G, Sadeghi M, Zeigler DR, Rahimian H, Ghandili S, Naghibzadeh N, Dehestani A (2011) First report of a bifunctional chitinase/ lysozyme produced by Bacillus pumilus SG2. Enzyme Microb Technol 48:225–231
40. García-Fraga B, da Silva AF, López-Seijas J, Sieim C (2014) Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT395 in Escherichia coli. Appl Microbiol Biotechnol 98:2133–2143
41. Staufenberger T, Imhoff JF, Labes A (2012) First crenarchaeal chitinase found in Sulfolobus tokodaii. Microbiol Res 167:262–269
42. Casados-Vázquez LE, Avila-Cabrera S, Bideshi DK, Barboza-Corona JE (2014) Heterologous expression, purification and biochemical characterization of endochitinase ChiA74 from Bacillus thuringiensis. Protein Expression Purif Doi: 10.1016/j.pep.2014.11.015
43. Lonhienne T, Mavromatis K, Vorgias CE, Buchon L, Gerday C, Bouriotis V (2011) Cloning, sequences, and characterization of two chitinase gene from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes. J Bacteriol 183:1773–1779
44. Ashry ESHE, Aly MRE (2007) Synthesis and biological relevance of N-acetylglucosamine-containing oligosaccharides. Pure Appl Chem 12:2229–2242
45. Chen JK, Shen CR, Liu CL (2010) N-acetylglucosamine: production and applications. Mar Drugs 8:2493–2516
46. Dube B, Lüke HJ, Aumailley M, Prehm P (2001) Hyaluronan reduced migration and proliferation in CHO cells. Biochim Biophys Acta 1538:283–289
47. Chien LJ, Lee CK (2007) Hyaluronic acid production by recombinant Lactococcus lactis. Appl Microbiol Biotechnol 77:339–346
48. Chien LJ, Lee CK (2007) Enhanced hyaluronic acid production in Bacillus subtilis by coexpressing bacterial hemoglobin. Biotechnol Progr 23:1017–1022
49. Danishefsky I, Steiner H, Bella A, Friedlander A (1969) Investigations on the chemistry of heparin: VI position of the sulfate ester groups. J Biol Chem 244:1741–1745
50. Bhavanandan VP, Meyer K (1966) Mucopolysaccharides: N-acetylglucosamine-and galactose-6-sulfates from keratosulfate. Science 151:1404–1405
51. Tsai M, Takeishi T, Thompson H, Langley KE, Zsebo KM, Metcalfe DD, Geissler EN, Galli SJ (2001) Induction of mast cell proliferation, maturation, and protein synthesis by the rat c-kit ligand, stem cell factor. Proc Natl Acad Sci USA 88(14):6382–6386
52. Ugorski M, Laskowska A (2002) Sialyl Lewis (a): a tumor-associated carbohydrate antigen involved in adhesion and metastatic potential of cancer cells. Acta Biochim Pol 49:303–311
53. Polley MJ, Phillips ML, Wayner E, Nudelman E, Singhal AK, Hakomori S, Paulson JC (1991) CD62 and endothelial cell-leukocyte adhesion molecule 1 (ELAM-1) recognize the same carbohydrate ligand, sialyl-Lewis x. Proc Natl Acad Sci USA 88:6224–6228
54. Piacente F, Bernardi C, Marin M, Blanc G, Abergel C, Tonetti MG (2013) Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus. Glycobiology. doi:10.1093/glycob/cwt089
55. Vimr E, Lichtenteiger C (2002) To sialylate, or not to sialylate: that is the question. Trends Microbiol 10:254–257
56. Kang JH, Gu PF, Wang Y, Li YK, Yang F, Wang Q, Qi QS (2012) Engineering of an N-acetylneuraminic acid synthetic pathway in Escherichia coli. Metab Eng 14:623–629
57. Song MC, Kim E, Ban YH, Yoo YJ, Kim EJ, Park SR, Pandey RP, Sohng JK, Yoon YJ (2013) Achievements and impacts of glycosylation reactions involved in natural product biosynthesis in prokaryotes. Appl Microbiol Biotechnol. doi:Doi:10.1007/s00253-013-4978-7
58. Hjort K, Presti H, Elväng A, Marinelli F, Sjöling S (2014) Bacterial chitinase with phytopathogen control capacity from suppressive soil revealed by functional metagenomics. Appl Microbiol Biotechnol 98:2819–2828
59. Schmeisser C, Steele H, Streit WR (2007) Metagenomics, biotechnology with non-culturable microbes. Appl Microbiol Biotechnol 75:955–962
60. Vaaje-Kolstad G, Westereng B, Horn SJ, Liu Z, Zhai H, Sørlie M, Eijsink VGH (2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330(6001):219–222
61. Wang M, Si T, Zhao HM (2012) Biocatalyst development by directed evolution. Bioresour Technol 115:117–125
62. Liang C, Firoroni M, Rodríguez-Ropero F, Xue Y, Schwaneberg U, Ma Y (2011) Directed evolution of a thermophilic endoglucanase (Cel5A) into highly active Cel5A variants with an expanded temperature profile. J Biotechnol 154:46–53
63. Fan YH, Fang WG, Xiao YH, Yang XY, Zhang YJ, Bidochka MJ, Pei Y (2007) Directed evolution for increased chitinase activity. Appl Microbiol Biotechnol 76:135–139