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Bio-Design and Manufacturing  2018 Vol.3 No.1 P.106~112


Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC

Author(s):  SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong

Affiliation(s):  Feed Science Institute of Animal Science College, Zhejiang University, Hangzhou 310029, China

Corresponding email(s):   jyisun@mail.hz.zj.cn

Key Words:  Trichoderma reesei, &beta, -glucanase, purification and characterization, stability

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SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong. Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC[J]. Journal of Zhejiang University Science D, 2018, 3(1): 106~112.

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author="SUN Jian-yi, LI Wei-fen, XU Zi-rong, GU Sai-hong",
journal="Journal of Zhejiang University Science D",
publisher="Zhejiang University Press & Springer",

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%A LI Wei-fen
%A XU Zi-rong
%A GU Sai-hong
%J Journal of Zhejiang University SCIENCE D
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%P 106~112
%@ 1869-1951
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%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2002.0106

T1 - Purification and some properties of a β-glucanase from a strain, Trichoderma reesei GXC
A1 - SUN Jian-yi
A1 - LI Wei-fen
A1 - XU Zi-rong
A1 - GU Sai-hong
J0 - Journal of Zhejiang University Science D
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SP - 106
EP - 112
%@ 1869-1951
Y1 - 2018
PB - Zhejiang University Press & Springer
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DOI - 10.1631/jzus.2002.0106

&beta;-glucanase was purified from a solid-state culture of Trichoderma reesei on wheat bran in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The molecular mass was determined to be 35.21 kilodaltons by sodium dodecyl sulfate-12.5% polyacrylamide gel electrophoresis. The &beta;-glucanase at low pHs was more stable than that at high pHs, and optimum pH was 5.0. The optimum temperature was 60 °C, and &beta;-glucanase was relatively stable at below 40 °C for 60 min. The Km of the enzyme on &beta;-glucan was 10.86 mg/ml, and the Vmax on &beta;-glucan was 14286 μmol of glucose equivalents per mg of the pure enzyme per min. The &beta;-glucanase activity was significantly inhibited by Fe3+ ions, and was reduced in the presence of Cu2+ ions, Mn2+ ions and Mg2+ ions at 5 mmol/L and 10 mmol/L, respectively. The &beta;-glucanase activity was stimulated by Co2+ ions, Ca2+ ions, Zn2+ ions, and Fe2+ ions at 1 mmol/L and 5 mmol/L, respectively.

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[1] Anderson,M.A., Stone,B.A., 1975. A new substrate for investigating the specificity of β- glucan hydrolases. FEBS Lett. 52:202-207.

[2] Borriss,R., Olsen,O., Thomsen,K.K., et al., 1989. Hybrid bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products. Carlsberg Res Commun; 54(2):41-54.

[3] Borriss,R., Buettner,K., Maentsaelae,P., 1990. Structure of the β-1,3-1,4-glucanase gene of Bacillus macerans: homologies to other beta-glucanases. Mol. Genet. 222:278-283.

[4] Bradford,M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 72:248-254.

[5] Brenes,A., Smith,M., Guenter,W., et al., 1993. Effect of enzyme supplementation on the performance parameters and digestive tract size of broiler chickens fed wheat- and barley- based diets. Poultry Science 72:1731-1739.

[6] Broz,J., Perrin,V., 1994. Dose related efficiency of Trichoderm viride enzyme complex on performance of broiler chickens receiving pelleted feeds. Archives Geflugelk 58:182-185.

[7] Buliga,G.S., Brant,D.A., Fincher,G.B., 1986. The sequence statistics and solution conformation of a barley (1→3,1→4)-β-D-glucan. Carbohydr. Res. 157:139-156.

[8] Chen,H., Li,X.L., Ljungdahl,L.G., 1997. Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin. J Bacteriol Oct. 179(19):6028-6034.

[9] Erfle,J.D., Teather,R.M., Wood,P.J., et al., 1988. Purification and properties of a 1,3-1,4-beta-D- glucanase (lichenase, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC from Bacteroides succinogenes cloned in Escherichia coli. Biochem J Nov 1;255(3):833-841.

[10] Ezio,A.M., Edward,A.H., Edward,L.R., 1961. Enzymatic Properties of a β-glucanase from Bacillus subtilis. The Journal of Biological Chemistry. 236(11):2858-2862.

[11] Fincher,G.B., Stone,B.A., 1986. Cell walls and their components in cereal grain Technology. Recent Adv. Cereal Grain Technol. 8: 207-293.

[12] Fleming,M., Kawakami,K., 1977. Studies of the fine structure of β-D-glucans of barleys extractted at different temperatures. Carbohydr. Res. 57:15-23.

[13] Gosalbes,M. J., Perez-Gonzalez,J.A., Navarro,A., 1991. Two β-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression and sequence analysis of genes encoding a xylanase and an endo-β-(1,3)-(1,4)-glucanase. J. Bacteriol. 173:7705-7710.

[14] Hofemeister,J., Kurtz,A., Borriss,R., et al., 1986. The β-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of Bacillus subtilis. Gene 49:177-187.

[15] Jensen,M.S., Thaela,M.J., Pierzynowski,S.G., 1996. Exocrine pancreatic secretion in young pigs fed barley-based diets supplemented with beta-glucanase. Journal of Animal Physiology and Animal Nutrition. 75:231-241.

[16] Laemmli,U.K., 1970. Detection of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227:680-685.

[17] Lloberas,J., Perez-pons,J.A., Querol,E., 1991. Molecular cloning, expression and nucleotide sequence of the endo-β-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Eur. J. Biochem. 197:337-343.

[18] Louw,M.E., Reid,S.J., Watson,T.G., 1993. Characterization, cloning and sequencing of a thermostable endo-(1,3-1,4) beta-glucanase-encoding gene from an alkalophilic Bacillus brevis. Appl Microbiol Biotechnol Jan.38(4):507-513.

[19] Miller,G.L., 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31:426-428.

[20] Murphy,N., McConnell,D.J., Cantwell,B.A., 1984. The DNA sequence of the gene and genetic control sites for the excreted B. subtilis enzyme β-glucan. hydrolase. Nucleic Acids Res. 12:5355-5367.

[21] Partrige,G., Wyatt,G., 1995. More flexibility with new generation of enzymes. World Poultry. 11(4):17-21.

[22] Schimming,S., Schwarz,W.H., Staudenbauer,W.L., 1991. Properties of a thermoactive beta-1,3-1,4-glucanase (lichenase) from Clostridium thermocellum expressed in Escherichia coli. Biochem Biophys Res Commun May 31.177(1):447-452.

[23] Sharma,A., Nakas,J.P., Sharma,A., et al., 1987. Preliminary Characterization of Laminarinase from Trichoderma Longibrachiatum. Enzyme Microb. Technol. 9. 89-93.

[24] Spilliaert,R., Hreggvidsson,G.O., Kristjansson,J.K., 1994, Cloning and sequencing of a Rhodothermus marinus gene, bglA, coding for a thermostable beta-glucanase and its expression in Escherichia coli. Eur J Biochem.224(3):923-930

[25] Tabernero,C., Coll,P.M., Fernandez-Abalos,J.M., 1994. Cloning and DNA sequencing of bgaA, a gene encoding an endo-beta-1,3-1,4-glucanase, from an alkalophilic Bacillus strain (N137). Appl Environ Microbiol. Apr.60(4):1213-1220.

[26] Viveros,A., Brenes,A., Pizarro,M., et al., 1994. Effect of enzyme supplementation of a diet based on barley and autoclave treatment on apparent digestibility, growth performance and gut morphology of broilers. Animal Feed Science and Technology. 48:237-251

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