$\require{mediawiki-texvc}$

연합인증

연합인증 가입 기관의 연구자들은 소속기관의 인증정보(ID와 암호)를 이용해 다른 대학, 연구기관, 서비스 공급자의 다양한 온라인 자원과 연구 데이터를 이용할 수 있습니다.

이는 여행자가 자국에서 발행 받은 여권으로 세계 각국을 자유롭게 여행할 수 있는 것과 같습니다.

연합인증으로 이용이 가능한 서비스는 NTIS, DataON, Edison, Kafe, Webinar 등이 있습니다.

한번의 인증절차만으로 연합인증 가입 서비스에 추가 로그인 없이 이용이 가능합니다.

다만, 연합인증을 위해서는 최초 1회만 인증 절차가 필요합니다. (회원이 아닐 경우 회원 가입이 필요합니다.)

연합인증 절차는 다음과 같습니다.

최초이용시에는
ScienceON에 로그인 → 연합인증 서비스 접속 → 로그인 (본인 확인 또는 회원가입) → 서비스 이용

그 이후에는
ScienceON 로그인 → 연합인증 서비스 접속 → 서비스 이용

연합인증을 활용하시면 KISTI가 제공하는 다양한 서비스를 편리하게 이용하실 수 있습니다.

초록
AI-Helper 아이콘AI-Helper

Chitin deacetylase(CDA; EC 3.5.1.41)는 키틴의 N-acetamide bonds를 가수분해하여 이를 키토산으로 전환시키는 효소다. 한편, 키토산은 의약, 화장품, 식품, 농업 등의 분야에서 다양하게 응용되는 고분자 다당류이다. 본 논문에서는 미생물 유래 CDA의 분포, 분석법, 효소적 특성, 기질 특이성, 작용기작, 유전자의 구조, 생물학적 역할, 응용 등의 최신 지견을 기술하고자 하였다. 미생물 CDA가 세포벽 형성과 식물-미생물 상호작용에 관여한다는 연구결과들을 제시하였으며, CDA의 유전자 구조를 다양한 acetylated poly/oligo-saccharides를 탈아세틸화하는 family 4 carbohydrate esterase의 유전자 구조와 비교하였다. 키틴의 탈아세틸화로 키토산을 제조하는 과정에 CDA의 활용 가능성과, CDA를 포함한 고활성의 키틴 대사효소들을 분비하는 곤충 병원균의 활용 가능성도 살펴보았다.

Abstract AI-Helper 아이콘AI-Helper

Chitin deacetylase (CDA; EC 3.5.1.41) catalyzes the hydrolysis of N-acetamide bonds of chitin, converting it to chitosan. Chitosan has several applications in areas such as biomedicine, food ingredients, cosmetics, pharmaceuticals, and agriculture. In this paper, occurrence, assay and purification p...

참고문헌 (52)

  1. Alfonso, C., O.M. Nuero, F. Santamaria, and F. Reyes. 1995. Purification of a heat stable chitin deacetylase from Aspergillus nidulans and its role in cell wall degradation. Curr. Microbiol. 30: 49-54 

  2. Araki, Y. and E. Ito. 1975. A pathway of chitosan formation in Mucor rouxii: enzymatic deacetylation of chitin. Eur. J. Biochem. 189: 249-253 

  3. Barber, M. S., R. E. Bertram, and J. P. Ride. 1989. Chitin oligosaccharides elicit lignification in wounded wheat leaves. Physiol, Mol. Plant Pathol. 34: 3-12 

  4. Bergmeyer, H.U. 1974. Method of Enzymatic Analysis, pp. 112-117. 2nd ed. Vol. 1, Verlag Chemie, Weinhein 

  5. Blair, D. E. and D. M. F. van Aalten. 2004. Structures of Bacillus subtilis PdaA, a family 4 cabohydrate esterase, and a complex with N-acetyl-glucosamine. FEBS Letters 570: 13-19 

  6. Caufrier, F., A. Martinou, C. Dupont, and V. Bouriotis. 2003. Carbohydrate esterase family 4 enzymes: substrate specificity. Carbohyd. Res. 338: 687-692 

  7. Chang, K. L., G. Tsai, J. Lee, and W.R. Fu. 1997. Heterogeneous N-deacetylation of chitin in alkaline solution. Carbohydro Res. 303: 327-332 

  8. Christodoulidou, A., V. Bouriotis, and G. Thireos. 1996. Two sporulation-specific chitin deacetylase-encoding genes are required for the ascospore wall rigidity of Saccharomyces cerevisiae. J. Biol. Chem. 271: 31420-31425 

  9. Christodoulidou, A., P. Briza, A. Ellinger, and V. Boriotis. 1999. Yeast ascospore wall assembly requires two chitin deacetylase isozymes. FEBS Lett. 460: 275-279 

  10. Davis, L. L. and S. Bartnicki-Garcia, 1984. Chitosan synthesis by the tandem action of chitin synthase and chitin deacetylase from Mucor rouxii. Biochemistry 23: 1065-1073 

  11. Deising, H. and J. Seigrist. 1995. Chitin deacetylase activity of the rust Uromyces viciae-fabaeis controlled by fungal morphogenesis. FEMS Microbiol. Lett. 127: 207-212 

  12. Denarie, J., F. Debelle, and J. C. Prome. 1996. Rhizobium lipo-chitooligosaccharide nodulation factors: signaling molecules mediating recognition and morphogenesis. Annu. Rev. Biochem. 65 : 503-535 

  13. Fernandes, A, M. G A Fontes, H. J. Gilbert, G. P. Hazlewood, T. H. Fernandes, and L. M. A. Ferreira. 1999. Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes. Biochem. J. 342: 105-110 

  14. Freiberg, C, R. Fellay, A. Bairoch, W. J. Broughton, A. Rosental, and X. Perret. 1997. Molecular basis of symbiosis between Rhizobium and legumes. Nature 387: 394-401 

  15. Gao, X., T. Katsumoto, and K. Onodera. 1995. Purification and characterization of chitin deacetylase from Absidia coerulea. J. Biochem. 117: 257-263 

  16. Fukushima, T., H. Yamamoto, A. Atrih, S. J. Foster, and J. Sekiguchi. 2002. A polysaccharide deacetylase gene(pdaa) is required for germination and for production of muramic delta-lactam residues in the spore cortex of Bacillus subtilis. J. Bacteriol. 184: 6007-6015 

  17. Goethalis, K., M. Gao, K. Tomekpe, M. V. Montagu, and M. Holsters. 1989. Common nodABC genes in Nod locus 1 of Arorhirobium caulinodans : nucleotide sequence and plantinducible expression. Mol. Gen. Genet. 219: 289-298 

  18. Hekmat, O., K. Tokuyasu, and S. G. Withers. 2003. Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS. Biochem. J. 374: 369-380 

  19. John, M., H. Rohrig, J. Schmidt, U. Wieneke, and J. Schell. 1993. Rhizobium NodB protein involved in nodulation signal synthesis is a chitooligosaccharide deacetylase. Proc. Natl. Acad. Sci. USA 90: 625-629 

  20. Kafetzopoulos, D., A. Martinou, and V. Bouriotis. 1993. Bioconversion of chitin to chitosan: purification and characterization of chitin deacetylase from Mucor rouxii. Proc. Natl. Acad. Sci. USA 90: 2564-2568 

  21. Kafetzopoulos, D., G Thireos, J. Voumakis, and V. Bouriotis. 1993. The primary structure of a fungal chitin deacetylase reveals the function for two bacterial gene products. Proc. Natl. Acad. Sci. USA 90: 8005-8008 

  22. Kauss, H. and B. Bauch. 1998. Chitin deacetylase from Colletotrichum lindemuthianum, pp. 518-523, In W. A Woods and S. T Kellogg. (eds.), Methods in Enzymology, vol. 161, Academic Press, San Diago 

  23. Kauss, H., W. Jeblick, and A. Domard. 1989. The degree of polymerization and N-acetylation of chitosan determines its ability to elicit callose formation in suspension cells and protoplast of Catharanthus roseus. Planta 178: 385-392 

  24. Laurie, J., J. H. Clarke, A. Ciruela, C. B. Faulds, G Williamson, H. J. Gilbert, J. E. Rixon, J. Millward-Sadler, and G. P. Hazlewood. 1997. The NodB domain of a multidomain xylanase from Cellulomonas fimi deacetylases acetylxylan. FEMS Microbiol. Lett. 148: 261-264 

  25. Martinou, A., D. Kafetzopoulos, and V. Bouriotis. 1993. Isolation of chitin deacetylase from Mucor rouxii by immunoaffinity chromatography. J. Chromatogr. 644: 35-41 

  26. Martinou, A., D. Kafetzopoulos, and V. Bouriotis. 1995. Chitin deacetylation by enzymatic means: monitoring of deacetylation processes. Carbohydr. Res. 273: 235-242 

  27. Martinou, A., V. Bouriotis, B. T. Stokke, and K. M. Varumd. 1998. Mode of action of chitin deacetylase from M. rouxii on partially N-acetylated chitosans. Carbohydr. Res. 311: 71-78 

  28. Martinou, A., D. Koutsioulis, and V. Bouritiotis. 2002. Expression, purification, and characterization of a cobalt-activated chitin deacetylase(Cda2p) from Saccharomyces cerevisiae. Prot. Expr. Purif. 24: 11l-116 

  29. Martinou, A., D. Koutsioulis, and V. Bouriotis. 2003. Cloning and expression of a chitin deacetylase gene(CDA2) from Saccharomyces cerevisiae in Escherichia coli . Purifiaction and characterization of the cobalt-dependent recombinant enzyme. Enzym. Microbial Technol 32: 757-763 

  30. Maw, T., T. K. Tan, E. Kohr, and S. M. Wong. 2002. Complete cDNA sequence of chitin deacetylase from Gongronella butleri and its phylogenetic analysis revealed clusters corresponding to taxonomic classification of fungi. J. Biosci. Bioeng. 93: 376-381 

  31. McMurrough, I., A. Flores-Carreon, and S. Bartnicki-Garcia. 1971. Pathway of chitin synthesis and cellular localization of chitin synthase in Mucor rouxii. J. Biol. Chem. 246: 3999-4007. 

  32. Mendgen, K., M. Hahn, and H. Deising. 1996. Morphogenesis and mechanisms of penetration by plant pathogenic fungi. Annu. Rev. Phytopathol. 34: 367-386 

  33. Nahar, P, Ghormade, V, and V. Deshpande. 2004. The extracellular constitutive production of chitin deacetylase in Metarhrlum anisopliae: possible edge to entomopathogenic fungi in the biological control of insect pests. J. Invertibrate Pathol 85: 80-88 

  34. Ohishi, K., K. Murase, T. Ohta, and H. Etoh. 2000. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90: 561-563 

  35. Sannan, T., K. Kurita, and Y. lwakura. 1976. Studies on chitin. Makromol Chem. 177: 3589-3600 

  36. Shrestha, B., K. Blondeau, W. F. Stevens, and F. L. Hegarat. 2004. Expression of chitin deacetylase from Colletotrichum lindemuthianum in Pichia pastoris: purification and characterization. Prot. Expr. Purif. 38: 196-204 

  37. Tokuyasu, K., M. Ohnishi-Kameyama, and K. Hayashi. 1996. Purification and characterization of extracellular chitin deacetylase from Colletotrichum lindemuthianum. Biosci. Biotechnol. Biochem. 60: 1598-1603 

  38. Tokuyasu, K., H. Ono, M. Ohnishi-Kameyama, K. Hayashi, and Y. Mori. 1997. Deacetylation of chitin oligosaccharides of dp 2-4 by chitin deacetylase from Colletotrichum lindemuthianum. Carbohydr. Res. 303: 353-358 

  39. Tokuyasu, K., H. Ono, K. Hayashi, and Y. Mori. 1999. Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis of ${\beta}-D-GlcNAc-(1{\to}4)-GlcN$ from chitobiose. Carbohydr. Res. 322:26-31 

  40. Tokuyasu, K., M. Ohnishi-Kameyama, K. Hayashi, and Y. Mori. 1999. Cloning and expression of chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum. J. Biosci. Bioeng. 87: 418-423 

  41. Tokuyasu, K., H. Ono, K. Hayashi, and Y. Mori. 1999. Reverse hydrolysis reaction of chitin deacetylase and enzymatic synthesis of $\beta -D-GlcNAc-(1\rightarrow 4)-GlcN$ from chitobiose. Carbohydr. Res. 322: 26-31 

  42. Tokuyasu, K., H. Ono, Y. Kitagawa, M. Ohnishi-Kameyama, K. Hayashi, and Y. Mori. 1999. Selective N-deacetylation of ${\rho}-nitrophenyl$ $N,N -diacetyl-{\beta} -chitobioside$ and its use to differentiate the action of two types of chitinases. Carbohydr. Res. 316: 173-178 

  43. Tokuyasu, K., H. Ono, M. Mitsutomi, K. Hayashi, and Y. Mori. 2000. Synthesis of a chitosan tetramer derivative, ${\beta}-D-GlcNAc-(1{\to} 4)-{\beta}-D-GlcNAc-(1{\to} 4)-{\beta}-D-GlcNAc-(1{\to} 4)-D-GlcN$ through a partial N-acetylation reaction by chitin deacetylase. Carbohydr. Res. 325: 211-215 

  44. Trudel, J. and A. Asselin. 1990. Detection of chitin deacetylase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 189: 249-253 

  45. Tsigos, A., K. Martinou, D. Varum, Kafetzopoulos, and A. Christodoulidou. 1994. Enzymatic deacetylation of chitin employing chitin deacetylases, pp. 98-107. In A. Kamicki et al.(eds.), Chitin World, Wirtschaftsverlag NW, Bremerhaven 

  46. Tsigos, I. and V. Bouriotis. 1995. Purification and characterization of chitin deacetylase from Colletotrichum lindemuthianum. J. Biol. Chem. 270: 26286-26291 

  47. Tsigos, I., N. Zydowicz, A. Martinou, A. Domard, and V. Bouriotis. 1999. Mode of action of chitin deacetylase from M. rouxii on N-acetylchitooligosaccharides. Eur. J. Biochem. 261: 1-9 

  48. Vander, P., K. M. Varum, A. Domard, N. E. Gueddari, and B. M. Moerschbacher. 1998. Comparison of the ability of partially acetylated chitosans and chitooligosaccharides to elicit resistance reactions in wheat leaves. Plant Physiol. 118: 1353-1359 

  49. Versali, M. F. and F. Cierisse. 1997. Expression and characterization of recombinant chitin deacetylase, pp. 273-278, In A. Domard et al.(eds.), Advances in Chitin Science, vol. 2, Jaques Andre Publisher 

  50. Vollmer, W. and A. Tomasz. 2000. The pgda gene encodes for a peptidoglycan N-acetylglucosarnine deacetylase in Streptococcus pneumoniae. J. Biol. Chem. 275: 20496-20501 

  51. Walker-Simons, M., D. Jin, C. A. West, L. Hadwiger, and C. A. Ryan. 1984. Comparison of proteinase inhibitor-inducing activities and phytoalexin elicitor activities of a pure fungal endopolygalacturonase, pectic fragments and chitosans. Plant Physiol. 76: 833-836 

  52. Yarnano, N., N. Oura, J. Wang, and S. Fujishima. 1997. Cloning and sequencing of the gene for N-acetylglucosamine use that contract divergent operons(nagE-nagAC) from Vibrio cholerae Non-I. Biosci. Biotech. Biochem. 61: 1349-1353 

저자의 다른 논문 :

관련 콘텐츠

저작권 관리 안내
섹션별 컨텐츠 바로가기

AI-Helper ※ AI-Helper는 오픈소스 모델을 사용합니다.

AI-Helper 아이콘
AI-Helper
안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

선택된 텍스트

맨위로