메뉴 건너뛰기




Volumn 72, Issue 12, 2008, Pages 3091-3099

Purification and characterization of chitinase isozymes from a red algae, Chondrus verrucosus

Author keywords

Chitinase; Cleavage pattern; Red algae; Seaweed; Substrate specificity

Indexed keywords

CHITIN; PHYTOPLANKTON; POLYSACCHARIDES; PURIFICATION; SEAWEED;

EID: 58149089174     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80141     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0013020634 scopus 로고    scopus 로고
    • Chitin: A biomaterial in waiting
    • Khor, E., Chitin: a biomaterial in waiting. Curr. Opin. Sol. State Mater. Sci., 6, 313-317 (2002).
    • (2002) Curr. Opin. Sol. State Mater. Sci , vol.6 , pp. 313-317
    • Khor, E.1
  • 2
    • 0038386053 scopus 로고    scopus 로고
    • Chitin: The undisputed biomolecule of great potential
    • Tharanathan, R. N., and Kittur, F. S., Chitin: the undisputed biomolecule of great potential. Crit. Rev. Food Sci. Nutr., 43, 61-87 (2003).
    • (2003) Crit. Rev. Food Sci. Nutr , vol.43 , pp. 61-87
    • Tharanathan, R.N.1    Kittur, F.S.2
  • 3
    • 33646145518 scopus 로고    scopus 로고
    • Substrate specificity of chitinases from two species of fish, greenling, Hexagrammos otakii, and common mackerel, Scomber japonicus, and the insect, tobacco hornworm, Manduca sexta
    • Matsumiya, M., Arakane, Y., Haga, A., Muthukrishnan, S., and Kramer, K. J., Substrate specificity of chitinases from two species of fish, greenling, Hexagrammos otakii, and common mackerel, Scomber japonicus, and the insect, tobacco hornworm, Manduca sexta. Biosci. Biotechnol. Biochem., 70, 971-979 (2006).
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 971-979
    • Matsumiya, M.1    Arakane, Y.2    Haga, A.3    Muthukrishnan, S.4    Kramer, K.J.5
  • 5
    • 0036311238 scopus 로고    scopus 로고
    • Characterization of 38 kDa and 42 kDa chitinase isozymes from the liver of Japanese squid Todarodes pacificus
    • Matsumiya, M., Miyauchi, K., and Mochizuki, A., Characterization of 38 kDa and 42 kDa chitinase isozymes from the liver of Japanese squid Todarodes pacificus. Fish. Sci., 68, 603-609 (2002).
    • (2002) Fish. Sci , vol.68 , pp. 603-609
    • Matsumiya, M.1    Miyauchi, K.2    Mochizuki, A.3
  • 6
    • 0037697492 scopus 로고    scopus 로고
    • Purification and some properties of a chitinase isozyme from the liver of Japanese common squid Todarodes pacificus
    • Matsumiya, M., Miyauchi, K., and Mochizuki, A., Purification and some properties of a chitinase isozyme from the liver of Japanese common squid Todarodes pacificus. Fish. Sci., 69, 427-429 (2003).
    • (2003) Fish. Sci , vol.69 , pp. 427-429
    • Matsumiya, M.1    Miyauchi, K.2    Mochizuki, A.3
  • 7
    • 0000749772 scopus 로고
    • Insect chitin: Physical state, synthesis, degradation and metabolic regulation
    • Kramer, K. J., and Koga, D., Insect chitin: physical state, synthesis, degradation and metabolic regulation. Insect Biochem., 16, 851-877 (1986).
    • (1986) Insect Biochem , vol.16 , pp. 851-877
    • Kramer, K.J.1    Koga, D.2
  • 8
    • 31444440508 scopus 로고    scopus 로고
    • Purification and characterization of a novel isozyme of chitinase from Bombyx mori
    • Kabir, K. E., Hirowatari, D., Watanabe, K., and Koga, D., Purification and characterization of a novel isozyme of chitinase from Bombyx mori. Biosci. Biotechnol. Biochem., 70, 252-262 (2006).
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 252-262
    • Kabir, K.E.1    Hirowatari, D.2    Watanabe, K.3    Koga, D.4
  • 9
    • 31444456022 scopus 로고    scopus 로고
    • Effect of Bombyx mori chitinase against Japanese pine sawyer (Monochamus alternatus) adults as a biopesticide
    • Kabir, K. E., Sugimoto, H., Tado, H., Endo, K., Yamanaka, A., Tanaka, S., and Koga, D., Effect of Bombyx mori chitinase against Japanese pine sawyer (Monochamus alternatus) adults as a biopesticide. Biosci. Biotechnol. Biochem., 70, 219-229 (2006).
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 219-229
    • Kabir, K.E.1    Sugimoto, H.2    Tado, H.3    Endo, K.4    Yamanaka, A.5    Tanaka, S.6    Koga, D.7
  • 10
    • 0028406304 scopus 로고    scopus 로고
    • Melchers, L. S., Apotheker-de, Groot, M., van der Knaap, J. A., Ponstein, A. S., Sela-Buurlage, M. B., Bol, J. F., Cornelissen, B. J., van den Elzen, Peter, J. M., and Linthorst, Huub, J. M., A new class of tobacco chitinases homologous to bacterial exo-chitinases displays antifungal activity. Plant J., 5, 469-480 (1994).
    • Melchers, L. S., Apotheker-de, Groot, M., van der Knaap, J. A., Ponstein, A. S., Sela-Buurlage, M. B., Bol, J. F., Cornelissen, B. J., van den Elzen, Peter, J. M., and Linthorst, Huub, J. M., A new class of tobacco chitinases homologous to bacterial exo-chitinases displays antifungal activity. Plant J., 5, 469-480 (1994).
  • 11
    • 0034169575 scopus 로고    scopus 로고
    • Comparison of chitinase isozymes from yam tuber: Enzymatic factor controlling the lytic activity of chitinases
    • Arakane, Y., Hoshika, H., Kawashima, N., Fujiya-Tsujimoto, C., Sasaki, Y., and Koga, D., Comparison of chitinase isozymes from yam tuber: enzymatic factor controlling the lytic activity of chitinases. Biosci. Biotechnol. Biochem., 64, 723-730 (2000).
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , pp. 723-730
    • Arakane, Y.1    Hoshika, H.2    Kawashima, N.3    Fujiya-Tsujimoto, C.4    Sasaki, Y.5    Koga, D.6
  • 12
    • 15244357854 scopus 로고    scopus 로고
    • Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf
    • Taira, T., Toma, N., and Ishihara, M., Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf. Biosci. Biotechnol. Biochem., 69, 189-196 (2005).
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 189-196
    • Taira, T.1    Toma, N.2    Ishihara, M.3
  • 13
    • 34848927821 scopus 로고    scopus 로고
    • Heterologous expression of new antifungal chitinase from wheat
    • Singh, A., Kirubakaran, S. I., and Sakthivel, N., Heterologous expression of new antifungal chitinase from wheat. Protein Expr. Purif., 56, 100-109 (2007).
    • (2007) Protein Expr. Purif , vol.56 , pp. 100-109
    • Singh, A.1    Kirubakaran, S.I.2    Sakthivel, N.3
  • 14
    • 34147138790 scopus 로고    scopus 로고
    • N-Acetylchitooligosaccharide is a potent angiogenic inhibitor both in vivo and in vitro
    • Wang, Z., Zheng, L., Yang, S., Niu, R., Chu, E., and Lin, X., N-Acetylchitooligosaccharide is a potent angiogenic inhibitor both in vivo and in vitro. Biochem. Biophys. Res. Commun., 357, 26-31 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.357 , pp. 26-31
    • Wang, Z.1    Zheng, L.2    Yang, S.3    Niu, R.4    Chu, E.5    Lin, X.6
  • 15
    • 0035675616 scopus 로고    scopus 로고
    • Oligosaccharide signaling for defence responses in plant
    • Shibuya, N., and Minami, E., Oligosaccharide signaling for defence responses in plant. Physiol. Mol. Plant Pathol., 59, 223-233 (2001).
    • (2001) Physiol. Mol. Plant Pathol , vol.59 , pp. 223-233
    • Shibuya, N.1    Minami, E.2
  • 16
    • 0021189336 scopus 로고
    • Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum
    • Kendra, D. F., and Hadwiger, L. A., Characterization of the smallest chitosan oligomer that is maximally antifungal to Fusarium solani and elicits pisatin formation in Pisum sativum. Exp. Mycol., 8, 276-281 (1984).
    • (1984) Exp. Mycol , vol.8 , pp. 276-281
    • Kendra, D.F.1    Hadwiger, L.A.2
  • 17
    • 1942504715 scopus 로고    scopus 로고
    • Moore, K. G., Price, M. S., Boston, R. S., Weissinger, A. K., and Payne, G. A., A chitinase from Tex6 maize kernels inhibits growth of Aspergillus flavus. Phytopathology, 94, 82-87 (2004).
    • Moore, K. G., Price, M. S., Boston, R. S., Weissinger, A. K., and Payne, G. A., A chitinase from Tex6 maize kernels inhibits growth of Aspergillus flavus. Phytopathology, 94, 82-87 (2004).
  • 18
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 19
    • 0001616015 scopus 로고
    • Comparative biochemistry of chitinases-anomeric form of the reaction products
    • Fukamizo, T., Koga, D., and Goto, S., Comparative biochemistry of chitinases-anomeric form of the reaction products. Biosci. Biotechnol. Biochem., 59, 311-313 (1995).
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 311-313
    • Fukamizo, T.1    Koga, D.2    Goto, S.3
  • 20
    • 0001199167 scopus 로고    scopus 로고
    • HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme
    • Koga, D., Yoshioka, T., and Arakane, Y., HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme. Biosci. Biotechnol. Biochem., 62, 1643-1646 (1998).
    • (1998) Biosci. Biotechnol. Biochem , vol.62 , pp. 1643-1646
    • Koga, D.1    Yoshioka, T.2    Arakane, Y.3
  • 21
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema, J. J., Structural features of plant chitinases and chitin-binding proteins. FEBS Lett., 350, 159-163 (1994).
    • (1994) FEBS Lett , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 22
    • 0041350490 scopus 로고    scopus 로고
    • Plant chitinase as a possible biocontrol agent for use instead of chemical fungicides
    • Karasuda, S., Tanaka, S., Kajihara, H., Yamamoto, Y., and Koga, D., Plant chitinase as a possible biocontrol agent for use instead of chemical fungicides. Biosci. Biotechnol. Biochem., 67, 221-224 (2003).
    • (2003) Biosci. Biotechnol. Biochem , vol.67 , pp. 221-224
    • Karasuda, S.1    Tanaka, S.2    Kajihara, H.3    Yamamoto, Y.4    Koga, D.5
  • 23
    • 0001678271 scopus 로고
    • Distribution of chitinolytic enzymes in seaweeds
    • Sekiguchi, J., Matsumiya, M., and Mochizuki, A., Distribution of chitinolytic enzymes in seaweeds. Fish. Sci., 61, 876-881 (1995).
    • (1995) Fish. Sci , vol.61 , pp. 876-881
    • Sekiguchi, J.1    Matsumiya, M.2    Mochizuki, A.3
  • 24
    • 77957071226 scopus 로고
    • Preparation of crustacean chitin
    • eds. Wood, W. A, and Kellog, S. T, Academic Press, New York, pp
    • Shimahara, K., and Takiguti, Y., Preparation of crustacean chitin. In "Methods in Enzymology" Vol. 161, eds. Wood, W. A., and Kellog, S. T., Academic Press, New York, pp. 417-423 (1988).
    • (1988) Methods in Enzymology , vol.161 , pp. 417-423
    • Shimahara, K.1    Takiguti, Y.2
  • 25
    • 77957063365 scopus 로고    scopus 로고
    • Ohtakara, A., Chitinase and β-N-acetylhexosaminidase from Pycnoporus cinnabarinus. In Methods in Enzymology 161, eds. Wood, W. A., and Kellog, S. T., Academic Press, New York, pp. 462-470 (1988).
    • Ohtakara, A., Chitinase and β-N-acetylhexosaminidase from Pycnoporus cinnabarinus. In "Methods in Enzymology" Vol. 161, eds. Wood, W. A., and Kellog, S. T., Academic Press, New York, pp. 462-470 (1988).
  • 26
    • 0029107764 scopus 로고
    • Baculovirus-mediated expression of a Manduca sexta chitinase gene: Properties of the recombinant protein
    • Gopalakrishnan, B., Muthukrishnan, S., and Kramer, K. J., Baculovirus-mediated expression of a Manduca sexta chitinase gene: properties of the recombinant protein. Insect Biochem. Mol. Biol., 25, 255-265 (1995).
    • (1995) Insect Biochem. Mol. Biol , vol.25 , pp. 255-265
    • Gopalakrishnan, B.1    Muthukrishnan, S.2    Kramer, K.J.3
  • 27
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., and Yagishita, K., A simple activity measurement of lysozyme. Agric. Biol. Chem., 33, 1154-1156 (1971).
    • (1971) Agric. Biol. Chem , vol.33 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 78651153791 scopus 로고
    • Disk electrophoresis. II. Method and application to human serum protein
    • Davis, B. J., Disk electrophoresis. II. Method and application to human serum protein. Ann. NY Acad. Sci., 121, 404-427 (1964).
    • (1964) Ann. NY Acad. Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379 (1987).
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 32
    • 0025689657 scopus 로고
    • Production and separation of peptides from proteins stained with Coomassie Brilliant blue R-250 after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kawasaki, H., Emori, Y., and Suzuki, K., Production and separation of peptides from proteins stained with Coomassie Brilliant blue R-250 after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal. Biochem., 191, 332-336 (1990).
    • (1990) Anal. Biochem , vol.191 , pp. 332-336
    • Kawasaki, H.1    Emori, Y.2    Suzuki, K.3
  • 33
    • 51249177164 scopus 로고
    • A method for preparing proteins and peptides for microsequencing
    • Jahnen-Dechent, W., and Simpson, R. J., A method for preparing proteins and peptides for microsequencing. Plant Mol. Biol. Rep., 8, 92-103 (1990).
    • (1990) Plant Mol. Biol. Rep , vol.8 , pp. 92-103
    • Jahnen-Dechent, W.1    Simpson, R.J.2
  • 34
    • 0031769523 scopus 로고    scopus 로고
    • Pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Pyrococcus furiosus: Cloning and overexpression in Escherichia coli of the gene, and its application to protein sequence analysis
    • Tsunasawa, S., Nakamura, S., Tanigawa, T., and Kato, I., Pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Pyrococcus furiosus: cloning and overexpression in Escherichia coli of the gene, and its application to protein sequence analysis. J. Biochem., 124, 778-783 (1998).
    • (1998) J. Biochem , vol.124 , pp. 778-783
    • Tsunasawa, S.1    Nakamura, S.2    Tanigawa, T.3    Kato, I.4
  • 35
    • 0024279561 scopus 로고
    • A new photosystem II reaction center component (4.8 kDa protein) encoded by chloroplast genome
    • Ikeuchi, M., and Inoue, Y., A new photosystem II reaction center component (4.8 kDa protein) encoded by chloroplast genome. FEBS Lett., 241, 99-104 (1988).
    • (1988) FEBS Lett , vol.241 , pp. 99-104
    • Ikeuchi, M.1    Inoue, Y.2
  • 39
    • 0031718988 scopus 로고    scopus 로고
    • Early events in the elicitation of plant defence
    • Ebel, J., and Mithöfer, A., Early events in the elicitation of plant defence. Planta, 206, 335-348 (1998).
    • (1998) Planta , vol.206 , pp. 335-348
    • Ebel, J.1    Mithöfer, A.2
  • 40
    • 0000538103 scopus 로고
    • Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: Induction of extracellular alkalinization, changes in protein phosphorylation, and establishment of a refractory state
    • Felix, G., Regenass, M., and Boller, T., Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: induction of extracellular alkalinization, changes in protein phosphorylation, and establishment of a refractory state. Plant J., 4, 307-316 (1993).
    • (1993) Plant J , vol.4 , pp. 307-316
    • Felix, G.1    Regenass, M.2    Boller, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.