Isolation, purification and partial characterization of the 2N2acetyl2D2 glucosaminidase from the pupae of Helicoverpa armigera
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- Φιλύρη Μαρκόπουλος
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1 Acta Entomologica Sinica, August 2005, 48 (4) : ISSN N2 2 2D2 1, 2, 1, 2, 1 3 (1.,, ; 2.,, ) : Helicoverpa armigera, Sephadex G2200 DEAE232, N2 2 2D UΠmg 2 N2 2 2D2 (pnp2 2D2GlcNAc), : ph 5163, 55 ph 4 8, ph > 8 ; min,, 50,, K m 0116 mmolπl, V m mol L - 1 min - 1 pnp2 2D2GlcNAc kjπmol : ; N2 2 2D2 ; ; ; : Q965 : A : (2005) Isolation, purification and partial characterization of the 2N2acetyl2D2 glucosaminidase from the pupae of Helicoverpa armigera HUANG Xiao2Hong 1, CHEN Qing2Xi 2, YOU Min2Sheng 1, WANG Jun 2, GUAN Xiong 1 3 ( 11 Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, College of Animal Science, Fujian Agriculture and Forestry University, Fuzhou , China ; 21 Key Laboratory of Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Xiamen, Fujian , China) Abstract: 2N2acetyl2D2glucosaminidase ( EC ) was purified from the pupae of ammonium sulfate fractionation and chromatography on Sephadex G2200 and DEAE2cellulose. Helicoverpa armigera by The purified enzyme preparation was homogeneous as judged by polyacrylamide gel electrophoresis. It was found that the specific activity of the enzyme was UΠmg. The optimal ph value was 5163 and the optimal temperature 55. The enzyme was stable in the ph ranges of 4 to 8 under 37. The enzyme follows typical Michaelis2Menten kinetics for the hydrolysis of pnp2 2D2GlcNAc and the K m and V m values were 0116 mmolπl and mol L - 1 min - 1, respectively. The activation energy of the enzyme for the hydrolysis of pnp2 2D2GlcNAc was kjπmol. Key words : Helicoverpa armigera ; 2N2acetyl2D2glucosaminidase ; isolation and purification ; kinetics ; stability N2 2 2D2 ( 2N2acetyl2D2 glucosaminidase, NAG, EC ) 3, ( Koga et al., 1987 ; Spindler and Buchholz,1988 ;Joshi et al., 1989 ; Kono et al., 1990 ; Broadway et al., 1995), NAG 21,42 N2 2D2,, (,2001),, NAG, : (2002AA245011) ; (2002N004) :,, ,,,,,E2mail : sina. com 3 Author for correspondence,e2mail : Received : ; Accepted :
2 4 : N2 2 2D2 499,, ; (,2000 ;,2001) Helicoverpa armigera, 20 90,,,, NAG,,,, 1 111, 2N2 2 2D2 (pnp2 2D2GlcNAc) ;Sephadex G2200 Pharmacia ;DEAE2cellulose232 Whatman ; ; : NAG, 30 % 70 %, Sephadex G2200, 0101 molπl ph 618 ( 012 molπl NaCl), 216 cm 60 cm, 8 mlπ h,, 210 mlπ DEAE2 32, NaCl (0 112 molπl) 0101 molπl ph cm 30 cm, 12 mlπh,,310 mlπ, NAG : Lin (2003) pnp2 2D2GlcNAc, 2 ml ( 011 molπl ph 5163,012 mmolπl ), L, 10 min, 2 ml 015 molπl NaOH Backman DU nm (OD 405 nm ) (pnp), L mol - 1 cm - 1 (U) :, 1 mol pnp : Folin2 (Lowry et al., 1951), : pnp2 2D2GlcNAc :,,, Lineweaver2Burk, ( V m ), V m, Arrhenius, (lgv m ) 1ΠT,, pnp2 2D2GlcNAc NAG 1 Sephadex G DEAE ( 1), UΠmg ( 2) 212 ph 37, ph, ph pnp2 2D2 GlcNAc ( 3) ph, ph ph, 30 min, 20 L ph 5163, ph, ( 3) ph 4 8, ph 4 ph 8
3 500 Acta Entomologica Sinica 48 1 N2 2 2D2 Sephadex G2200 (A) DEAE232 (B) Fig. 1 Purification chromatography of the 2N2acetyl2D2glucosaminidase on Sephadex G2200 (A) and on DEAE2cellulose (B) 1 N2 2 2D2 Table 1 Purification of the 2N2acetyl2D2glucosaminidase from Helicoverpa armigera (ml) (mg) (U) (UΠmg) ( %) Purification Total volume Total protein Total activity Specific activity Recovery Purification factor Crude preparation % 70 % 30 % - 70 %(NH 4 ) 2 SO Sephadex G DEAE2cellulose N2 2 2D2 Fig. 2 SDS2PAGE of the purified 2N2 acetyl2d2glucosaminidase 214 ph molπl, 20 L ( 015 mgπml), ( 4),, (25 75 ) 30 min 3 ph N2 2 2D2 ph Fig. 3 The effect of ph on the activity and ph stability of 2N2acetyl2D2glucosaminidase 4 N2 2 2D2 Fig. 4 The effect of temperature on the activity and temperature stability of 2N2acetyl2D2glucosaminidase
4 4 : N2 2 2D2 501,, 20 L (ph 5163,37 ), ( 4) : min,, pnp2 2D2GlcNAc 2 ml ph 5163,, 37,, Michaelis2Menten ( 5 ) Lineweaver2Burk, pnp2 2D2GlcNAc K m V m 0116 mmolπl mol L - 1 min - 1 ( 5) 5 N2 2 2D2pNP 2 2D2GlcNAc Lineweaver2Burk Fig. 5 The Lineweaver2Burk plot of 2N2acetyl2D2 glucosaminidase for the hydrolysis of pnp2 2D2GlcNAc The inset shows the relationship between the initial rate and the substrate concentration. 217 pnp2 2D2GlcNAc pnp2 2D2GlcNAc V m Arrhenius, (lgv m ) 1ΠT, ( 6), pnp2 2D2GlcNAc kjπmol 3,,, 6 pnp2 2D2GlcNAc Fig. 6 Determination of the activation energy of 2N2acetyl2D2glucosaminidase for the hydrolysis of pnp2 2D2GlcNAc, N2 2 2D2 Sephadex G2200 DEAE232,N2 2 2D ,, 8016 % Koga (1986) DEAE Bio2Gel Sephacryl S2200 Bombyx mori N2 2 2D , % Koga,,,,,, NAG ph 5163,, ph 4 8 ( Koga et al.,1986),, ph (, 2004) Ohtakara ( 1979) Vibrio sp. ph 9 11,,,
5 502 Acta Entomologica Sinica ,,,, NAG K m 0116 mmolπl, ( Koga et al.,1986) NAG K m (01787 mmolπl) Penaeus vannamei K m (01254 mmolπl) (Xie et al.,2004), NAG pnp2 2 D2GlcNAc NAG, NAG, ( References) Broadway RM, Williams DL, Kain WC, Harman GE, Lorito M, Labeda DP, Partial characterization of chitinolytic enzymes from Streptomyces albidoflavus. Lett. Appl. Microbiol., 20 (5) : Huang XH, Chen QX, Wang J, Sha L, Huang ZP, Guan X, Isolation, purification and properties of the chitinase from Bacillus thuringiensis. Chin. J. Appl. Environ. Biol., 10 (6) : [,,,,,,20041 ( Bacillus thuringiensis).,10 (6) : ] Joshi S, Kozlowski M, Richens S, Comberbach DM, Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens. Enzyme Microb. Technol., 11(5) : Koga D, Shimazaki C, Yamamoto K, Inoue K, Kimura S, Ide A, N2acetyl2D2glucosaminidases from integument of the silkworm, Bombyx mori : comparative biochemistry with the pupal alimentary canal enzyme. Agric. Biol. Chem., 51 (6) : Koga D, Nakashima M, Matsukura T, Kimura S, Ide A, Purifications and properties of 2N2acetyl2D2glucosaminidase from alimentary canal of the silkworm, Bombyx mori. Agric. Biol. Chem., 50 (9) : Kono M, Matsui T, Shimizu C, Koga D, Purifications and some properties of chitinase from the liver of a prawn, Agric. Biol. Chem., 54(8) : Penaeus japonicus. Lin JC, Chen QX, Shi Y, Li SW, Zhao H, The chemical modification of the essential groups of 2N2acetyl2D2glucosaminidase from cornutus Solander. J. IUBMB Life, 55 (9) : Turbo Lowry OH, Rosebrough NJ, Farr AL, Randall RJ, Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193 : Otakara A, Mitsutomi M, Uchida Y, Purification and some properties of chitinase from Vibrio sp. J. Ferment. Technol., 57 (3) : Ouyang SW, Liu JL, Feng LX, Zhao KJ, Research on insect chitinases and their application. Journal of Mountain Agriculture and Biology, 20(2) : [,,,, , 20 (2) : ] Spindler KD, Buchholz F, Partial characterization of chitin degrading enzymes from two euphausiids, Euphausia superba and Meganyctiphanes norvegica. Polar Biol., 9 : Wu QJ, Zhang WJ, Zhang YJ, Insect chitinase and its potential use in plant protection. Entomological Knowledge, 37 (5) : [,,, , 37 (5) : ] Xie XL, Chen QX, Lin JC, Wang Y, Purification and some properties of 2N2acetyl2D2glucosaminidase from prawn ( Penaeus vannamei). Marine Biology, 146 (1) : ( : )
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