[en] This paper is the first to investigate the production and partial characterization of the chitinase enzyme from a moderately halophilic bacterium Planococcus rifitoensis strain M2-26, earlier isolated from a shallow salt lake in Tunisia. The impact of salt, salinity concentration, pH, carbon and nitrogen sources on chitinase production and activity have been determined. This is the first report on a high salt-tolerant chitinase from P. rifitoensis, since it was active at high salinity (from 5 to 30% NaCl) as well as in the absence of salt. This enzyme showed optimal activity at 70 C and retained up to 82 and 66% of its original activity at 80 or 90 C, respectively. The activity of the enzyme was also shown over a wide pH range (from 5 to 11). For characterization of the enzyme activity, the chitinase secreted in the culture supernatant was partially purified. The preliminary study of the concentrated dialysed supernatant on native PAGE showed at least three
chitinases produced by strain M2-26, with highest activity approximately at 65 kDa. Thus, the thermo-tolerant and high salt-tolerant chitinases produced by P. rifitoensis strain M2-26 could be useful for application in diverse areas such as biotechnology and agro-industry.
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Aunpad R, Panbangred W (2003) Cloning and Characterization of the Constitutively Expressed Chitinase C Gene from a Marine Bacterium, Salinivibrio costicola Strain 5SM-1. J Biosci and Bioeng 96(6): 529-536.
Barboza-Corona JE, Nieto-Mazzocco E, Velazquez-Robledo R, Salcedo-Hernandez R, Bautista M, Jimenez B, Ibarra JE (2003) Cloning, sequencing, and expression of the chitinase gene chiA74 from Bacillus thuringiensis. Appl Environ Microbiol 69(2): 1023-1029.
Chuan LD (2006) Review of fungal chitinases. Mycopathologia 161: 345-360.
Essghaier B, Fardeau ML, Cayol JL, Hajlaoui MR, Boudabous A, Jijakli H, Sadfi-Zouaoui N (2009) Biological control of grey mould in strawberry fruits by halophilic bacteria. J Appl Microbiol 106: 833-846.
Freeman S, Minzm O, Kolesnik I, Barbul O, Zveibil A, Maymon M, Nitzani Y, Kirshner B, Rav-David D, Bilu A, Dag A, Shafir S, Elad Y (2004) Trichoderma biocontrol of Colletotrichum acutatum and Botrytis cinerea and survival in strawberry. Eur Plant Pathol 110: 361-370.
Fujii T, Miyashita K (1993) Multiple domain structure in a chitinase gene (chic) of Streptomyceslividans. J Gen Microbiol 139: 677-686.
Gohel V, Maisuria V, Chhatpar HS (2007) Utilization of various chitinous sources for production of mycolytic enzymes by Pantoeadispersa in bench-top-fermenter. Enzyme Microb Technol 40: 1608-1614.
Gomez Ramirez M, Rojas Avelizapa LI, Rojas Avelizapa NG, Cruz Camarillo R (2004) Colloidal chitin stained with Remazol Brillant Blue R®, a useful substrate to select chitinolytic microorganisms and to evaluate chitinases. J Microbiol Methods 56: 213-219.
Gupta R, Saxena RK, Chaturvedi P, Virdi JS (1995) Chitinase production by Streptomycesvirdificans: its potential in fungal cell walls lysis. J Appl Bacteriol 78: 378-383.
Guthrie JL, Khalif S, Castle AJ (2005) An improved method for detection and quantification of chitinase activities. Can J Microbiol 51(6): 491-495.
Huang CJ, Wang TK, Chung SC, Chen CY (2005) Identification of an Antifungal Chitinase from a Potential Biocontrol Agent, Bacillus cereus 28-9. J Biochem Mol Biol 38(1): 82-88.
Laemmli UK (1970) Cleavage on struictural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
Leelasuphakul W, Sivanunsakul P, Phongpaichit S (2006) Purification, characterization and synergetic activity of β1, 3-glucanase and antibiotic extract from an antagonistic Bacillus subtilis NRS 89-24 against rice blast and sheath blight. Enzyme Microbiol Tech 38: 990-997.
Morimoto K, Karita S, Kimura T, Sakka K, Ohmiya K (1997) Cloning, Sequencing, and Expression of the Gene Encoding Clostridium paraputrificum Chitinase ChiB and Analysis of the Functions of Novel Cadherin-Like Domains and a Chitin-Binding Domain. J Bacteriol 179(23): 7306-7314.
Niehaus F, Bertoldo C, Kahler M, Antranikian G (1999) Extremophiles as a source of novel enzymes for industrial application. App Microbiol Biotechnol 51: 711-729.
Nielsen P, Sorensen J (1997) Multi-target and medium-independent fungal antagonism by hydrolytic enzymes in Paenibacillus polymyxa and Bacillus pumilus strains from barley rhizosphere. FEMS Microbiol Ecol 22: 183-192.
Pleban S, Chernin L, Shet I (1997) Chitinolytic activity of endophytic strain of Bacilluscereus. Lett Appl Microbiol 25: 284-288.
Rodriguez-Kabana R, Godoy G, Morgan-Jones G, Shelby RA (1983) the determination of soil chitinase activity: conditions for assay and ecological studies. Plant Soil 75: 95-106.
Rojas-Avelizapa LI, Cruz Camarillo R, Guerro MI, Rodriguez Vazquez R, Ibarra JE (1999) Selection and characterization of a proteo-chitinolytic strain of Bacillus thuringiensis, able to grow in shrimp waste media. World J Microbiol Biotechnol 15: 299-308.
Sadfi-zouaoui N, Essghaier B, Hannachi I, Hajlaoui MR, Boudabous A (2007) First report on the use of moderately halophilic bacteria against stem canker of greenhouse tomatoes caused by Botrytis cinerea. Ann Microbiol 57(3): 337-339.
Sadfi-Zouaoui N, Essghaier B, Hajlaoui MR, Fardeau ML, Cayol JL, Ollivier B, Boudabous A (2008) Ability of moderately halophilic bacteria to control Grey mould disease on tomato fruits. J Phytopathol 156: 42-52.
Sivitil AL, Kirchman DL (1998) A chitin-binding domain in a marine bacterial chitinase and other microbial chitinases: implications for the ecology and evolution of 1, 4-β-glycanase. Microbiology 144: 1299-1308.
Smaali MI, Gargouri M, Limam F, Fattouch S, Maugard T, Legoy MD, Marzouki N (2003) Production Purification and Biochemical Characterization of two β-Glucosidases from Sclerotiniasclerotiorum. Appl Biochem Biotechno1 11(1): 29-40.
Taylor G, Jabaji-hare S, Charest PM, Khan W (2002) Purification and characterization of an extracellular exochitinase, β-N-acdetylhexosaminidase, from the fungal mycoparasitte Stachybotryselegans. Can J Microbiol 48: 311-3119.
Thamthiankul S, Suan-Ngay S, Tantimavanich S, Panbangred W (2001) Chitinase from Bacillus thuringiensis subsp. Pakistani. Appl Microbiol Biotechnol 56: 396-401.
Trachuck LA, Revina LP, Shemyakina TM, Chestukhina GG, Stepanov VM (1996) Chitinases of Bacilluslicheniformis B6839: isolation and properties. Can J Microbiol 42: 307-315.
Tsujibo H, Minoura K, Miyamoto K, Endo H, Moriwaki M, Inamori Y (1993a) Purification and properties of a Thermostable Chitinase from Streptomyces thermoviolaceus OPC-520. Appl Environ Microbiol 59: 620-622.
Tsujibo H, Orikoshi H, Tanno H, Fujimoto K, Miyamoto K, Imada C, Okami Y, Inamori Y (1993b) Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J Bacteriol 175: 176-181.
Tsujibo H, Kondo N, Tanaka K, Miyamoto K, Baba N, Inamori Y (1999) Molecular analysis of the gene encoding a novel transglycosylative enzyme from Alteromonas sp strain O-7 and its physiological role in the chitinolytic system. J Bacteriol 181: 5461-5466.
Vaidya RJ, Shah IM, Vyas PR, Chhatpar HS (2001) Production of chitinase and optimization from a novel isolate Alcaligenesxylosoxydans: potential in antifungal biocontrol. Word J Microbiol Biotechnol 17: 691-696.
Vionis A, Niemeyer F, Karagouni AD, Schrempf H (1996) Production and processing of a 59 kDa exochitinase during growth of Streptomyces lividans pCHIO12 in soil microcosms amended with crab or fungal chitin. Appl Environ Microbiol 62: 1774-1780.
Wang SY, Moyne A, Thottappilly G, Wu S, Locy RD, Singh NK (2001) Purification and characterization of a Bacillus cereus exochitinase. Enzyme Microb Technol 28: 492-498.
Watanabe T, Oyanagi W, Suzuki K, Tanaka H (1990) Chitinase system Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J Bacteriol 172: 4017-4022.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.
