Multiple chitinases of an endophytic Serratia proteamaculans 568 generate chitin oligomers

Bioresource Technology

Volumn 112, Issue , 2012, Pages 261-269

  Purushotham, Pallinti ^a   Sarma, P V S R N ^a   Podile, Appa Rao ^a  

^a UNIVERSITY OF HYDERABAD   (India)

Author keywords

Chitin; Chitinases; Chitooligosaccharides; Serratia proteamaculans 568

Indexed keywords

3D MODELS; CHITINASES; CHITOOLIGOSACCHARIDES; COLLOIDAL CHITIN; END-PRODUCTS; HETEROLOGOUS EXPRESSION; POLYMERIC SUBSTRATE; SERRATIA PROTEAMACULANS; SERRATIA PROTEAMACULANS 568; SUBSTRATE SPECIFICITY; TETRAMERS;

DIMERS; SUBSTRATES;

CHITIN;

CHITINASE; DIMER; OLIGOMER; POLYMER; TETRAMER;

BACTERIUM; CHEMICAL BINDING; CHITIN; ENDOPHYTE; ENZYME ACTIVITY; GENE EXPRESSION; GENOME; SUBSTRATE;

ARTICLE; BACTERIAL GENE; BINDING KINETICS; ENTEROBACTERIACEAE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; INCUBATION TIME; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; SERRATIA PROTEAMACULAN 568;

BACTERIAL PROTEINS; CHITIN; CHITINASE; CLONING, MOLECULAR; COLLOIDS; ENDOPHYTES; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; OLIGOSACCHARIDES; SERRATIA; SOLUBILITY; SUBSTRATE SPECIFICITY; TEMPERATURE; TIME FACTORS;

SERRATIA PROTEAMACULANS;

EID: 84859218754     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2012.02.062     Document Type: Article

References (34)

1. Aam B.B., Heggset E.B., Norberg A.L., Sørlie M., Vårum K.M., Eijsink V.G.H. Production of chitooligosaccharides and their potential applications in medicine. Mar. Drugs. 2010, 8:1482-1517.
2. Chuang H.H., Lin H.Y., Lin F.P. Biochemical characteristics of C-terminal region of recombinant chitinase from Bacillus licheniformis-implication of necessity for enzyme properties. FEBS J. 2008, 275:2240-2250.
3. Divne C., Ståhlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K., Teeri T.T., Jones T.A. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 1994, 265:524-528.
4. ChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay. Arch. Biochem. Biophys. 2004, 426:286-297.
5. Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 1997, 7:637-644.
6. Horn, S.J., Sikorski, P., Cederkvist, J.B., Vaaje-Kolstad, G., Sørlie, M., Synstad, B., Vriend, G., Vårum, K.M., and Eijsink, V.G.H. 2006a. Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proc. Natl. Acad. Sci. USA. 103, 18089-18094.
7. Horn S.J., Sørbotten A., Synstad B., Sikorski P., Sørlie M., Vårum K.M., Eijsink V.G. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 2006, 273:491-503.
8. Huskisson E.C. Glucosamine and chondroitin for osteoarthritis. J. Int. Med. Res. 2008, 36:1161-1179.
9. Je J.Y., Kim S.K. Antioxidant activity of novel chitin derivative. Bioorg. Med. Chem. Lett. 2006, 16:1884-1887.
10. Kadokura K., Rokutani A., Yamamoto M., Ikegami T., Sugita H., Itoi S. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of hetero disaccharide from chitin. Microbiol. Biotechnol. 2007, 75:357-365.
11. Katouno F., Taguchi M., Sakurai K., Uchiyama T., Nikaidou N., Nonaka T., Sugiyama J., Watanabe T. Importance of exposed aromatic residues in chitinase B from Serratia marcescens 2170 for crystalline chitin hydrolysis. J. Biochem. 2004, 136:163-168.
12. Kim H.S., Timmis K.N., Golyshin N.P. Characterization of a chitinolytic enzyme from Serratia sp. KCK isolated from kimchi juice. Appl. Microbiol. Biotechnol. 2007, 75:1275-1283.
13. Mehmood M.A., Xiao X., Hafeez F.Y., Gai Y., Wang F. Purification and characterization of a chitinase from Serratia proteamaculans. World. J. Microbiol. Biotechnol. 2009, 25:1955-1961.
14. Nazari B., Saito A., Kobayashi M., Miyashita K., Wang Y., Fujii T. High expression levels of chitinase genes in Streptomyces coelicolor A3(2) grown in soil. FEMS Microbiol. Ecol. 2011, 77:623-635.
15. Neeraja C., Moerschbacher B., Podile A.R. Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13. Bioresour. Technol. 2010, 101:3635-3641.
16. Neeraja Ch., Anil K., Purushotham P., Suma K., Sarma P., Moerschbacher B.M., Podile A.R. Biotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants. Crit. Rev. Biotechnol. 2010, 30:231-241.
17. Okamoto Y., Yano R., Miyatake K., Tomohiro I., Shigemasa Y., Minami S. Effects of chitin and chitosan on blood coagulation. Carbohydr. Polym. 2003, 53:337-342.
18. Orikoshi H., Nakayama S., Hanato C., Miyamoto S., Tsujibo H. Role of the N-terminal polycystic kidney disease domain in chitin degradation by chitinase A from a marine bacterium, Alteromonas sp. strain O-7. J. Appl. Microbiol. 2005, 99:551-557.
19. Orikoshi H., Nakayama S., Miyamoto K., Hanato C., Yasuda M., Inamori Y., Tsujibo H. Roles of four chitinases (ChiA, ChiB, ChiC, and ChiD) in the chitin degradation system of marine bacterium Alteromonas sp. Strain O-7. Appl. Environ. Microbiol. 2005, 71:1811-1815.
20. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein?. Protein Sci. 1995, 4:2411-2423.
21. Papanikolau Y., Prag G., Tavlas G., Vorgias C.E., Oppenheim A.B., Petratos K. High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 2001, 40:11338-11343.
22. Perrakis A., Tews I., Dauter Z., Oppenheim A.B., Chet I., Wilson K.S., Vorgias C.E. Crystal structure of a bacterial chitinase at 2.3å resolution. Structure 1994, 2:1169-1180.
23. Salvatore S., Heuschkel R., Tomlin S., Davies S.E., Edwards S., Walker-Smith J.A., French I., Murch S.H. A pilot study of N-acetyl glucosamine, a nutritional substrate for glycosaminoglycan synthesis, in paediatric chronic inflammatory bowel disease. Aliment. Pharmacol. Ther. 2000, 14:1567-1579.
24. Suzuki K., Sugawara N., Suzuki M., Uchiyama T., Katouno F., Nikaidou N., Watanabe T. Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation. Biosci. Biotechnol. Biochem. 2002, 66:1075-1083.
25. Suzuki K., Taiyoji M., Sugawara N., Nikaidou N., Henrissat B., Watanabe T. The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases. Biochem. J. 1999, 343:587-596.
26. Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N., Barac T., Vangronsveld J., van der Lelie1 D. Genome survey and characterization of endophytic bacteria exhibiting a beneficial effect on growth and development of poplar trees. Appl. Environ. Microbiol. 2009, 75:748-757.
27. Terwisscha van Scheltinga A.C., Kalk K.H., Beintema J.J., Dijkstra B.W. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 1994, 2:1181-1189.
28. Uchiyama T., Katouno F., Nikaidou N., Nonaka T., Sugiyama J., Watanabe T. Roles of the exposed aromatic residues in crystalline chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem. 2001, 276:41343-41349.
29. Vaaje-Kolstad G., Westereng B., Horn S.J., Liu Z., Zhai H., Sørlie M., Eijsink G.V.H. An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 2010, 330:219-222.
30. van Aalten D.M.F., Komander D., Synstad B., Gåseidnes S., Peter M.G., Eijsink V.G.H. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc. Natl. Acad. Sci. USA 2001, 98:8979-8984.
31. van Aalten D.M.F., Synstad B., Brurberg M.B., Hough E., Riise B.W., Eijsink V.G.H., Wierenga R.K. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-å resolution. Proc. Natl. Acad. Sci. USA 2000, 97:5842-5847.
32. Watanabe T., Ito Y., Yamada T., Hashimoto M., Sekine S., Tanaka H. The roles of C-terminal domain and type III domains of chitinase A1 from Bacillus circulans WL-12 in chitin degradation. J. Bacteriol. 1994, 176:4465-4472.
33. Zakariassen H., Aam B.B., Horn S.J., Vårum K.M., Sørlie M., Eijsink V.G. Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency. J. Biol. Chem. 2009, 284:10610-10617.
34. Zou J., Kleywegt G.J., Stahlberg J., Driguez H., Nerinckx W., Claeyssens M., Koivula A., Teeri T.T., Jones T.A. Crystallogrphic evidence for substrate ring distortion and protein conformational changed during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei. Structure Fold Des. 1999, 15:1035-1045.