• 제목/요약/키워드: chitin degradation

검색결과 30건 처리시간 0.028초

카틴과 셀룰로우스의 복합체로부터 새로운 생체흡수성 봉합사의 개발 (Development of New Biocompatible Fiber form Composite of Chitin and Cellulose)

  • 이충우;홍영근이화섭윤정원
    • KSBB Journal
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    • 제8권3호
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    • pp.237-242
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    • 1993
  • Chitin 섬유는 인장강도가 기대치 보다 약하며 생 체조직 내에서 흡수도가 너무 빨라 수술 후 2주일 정도의 강도 유지밖에 못하는 단점 등이 었으므로, chitin과 그 구조가 비슷한 cellulose와 혼합하여 인 장력과 유연성이 크게 증대된 Chitulose 섬유를 개 발하였다. 우선 chitin과 cellulose가 잘 용해되어 혼 합펼 수 있는 용매로서 DMAc/LiCl을 탐색하였으며 이 용애계에 용해시킨 Chitulose 용액을 가지고 습 식방사하여 얻은 Chitulose 섬유 중, 용매에 대한 chitin cellulose 함량비가 1.5: 0.2얼 때, Instron 시험결과 강도와 유연성이 가장 좋았으며, 멸균시 autoclave해도 변화되지 않아 열에 매우 안정한 것 으로 나타났다. 이 섬유를 가지고 400-500g되는 백서의 피하조직에 매몰시킨 후, 생체 내 분해흡수 도를 관찰한 결과, 매볼 후 14일부터 분해되기 시작 하여 40일 후에는 완전히 분해흡수되였다.

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키틴 ${\cdot}$키토산 및 그 올리고당의 면역작용에 의한 항종양 활성 (Antitumor Activities by lmmunological Function of Chitin, Chitosan and Their Oligosaccharides)

  • 전유진;김세권
    • 생명과학회지
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    • 제7권2호
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    • pp.149-159
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    • 1997
  • Chitin, a linked polysaccharide composed of 2-acetamido-2-deoxy-$\beta$-D-glucopytanose residues, is distributed widely in nature. It has been utilized on various application field due to the development of chitin derivatives such as chitosan, partial deacetylated chitin, carboxylmethyl chitin, sulfated chitin, and so on. Chitin and chitosan have been recently interested in antitumor and antimicrobial activities, because of a powerful tumor inhibitory effect against experimental mouse tumors. Especially, the oligosaccharides obtained by partial degradation of them exhibited a remarkable antitumor effect against sarcoma 180, MM 48 and Meth Asolid tumors and antimetastatic effect against Lewis lung carcinoma in mice. This review describes on antitumor effects of chitin, chitosan and their oligosaccharides by their mechanism of action involving enhancement of immunological system.

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Serratia marcescens KFRI314 chitinase 유전자의 클로닝과 키틴분해에 관한 효소의 역할 (Cloning of Serratia marcescens KFRI314 chitinase genes and its role on chitin degradation)

  • 김정태;최신건
    • 산업기술연구
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    • 제30권B호
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    • pp.61-68
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    • 2010
  • Three chitinase genes (chiA, chiB, and chiC) were cloned into E. coli by PCR amplification from Serratia marcescens KFRI314. The sizes of cloned chitinase genes were 1692 bp, 1500 bp, and 1443 bp which correspond to 563, 499, and 480 amino acids, respectively. Recombinant chitinases were overexpressed using pHCEIA expression vector and purified to homogenity. The molecular weights of chitinases were about 60kDa, 50 kDa, 52 kDa, respectively. Optimum pHs were around pH 5~6 and optimum temperatures were $45{\sim}50^{\circ}C$ while 90% of enzyme activities were stable up to $50^{\circ}C$. The specific activities of ChiA, ChiB, and ChiC were 233.1, 278.8, $111.3{\mu}mol\;(min)^{-1}\;mg^{-1}$ against colloidal chitin. From experiments using TLC and fluorescent substrate analogues, it was demonstrated that ChiA was endo-chitinase while ChiB and ChiC were chitobiosidase.

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Statistical Optimization of Chitinase Production by Pantoea dispersa to Enhance Degradation of Crustacean Chitin Waste

  • GOHEL;VIPUL;DERICK JIWAN;PRANAV VYAS;H. S. CHHATPAR
    • Journal of Microbiology and Biotechnology
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    • 제15권1호
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    • pp.197-201
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    • 2005
  • A novel chitinase-producing bacterial strain of Pantoea dispersa was isolated from the sea near Bhavnagar, India for efficient disposal of chitinous waste from the seafood processing industry. The medium components were optimized by using a cubic model in the central composite design for increasing chitinase production. The optimal concentrations for higher production of chitinase were (g l-1) chitin, 10.0; urea, 0.35; MgSO4 7H2O, 0.08, and CaCl2, 0.15. Here, peptone (0.05 g l-1) was used as a constant variant in all trials. Using a statistical optimization method, the chitinase production was found to increase from 108 to 486.4 units ml-1. Chitin was prepared from the crustacean waste, and Fourier Transform Infrared (FTIR) Spectroscopy was used to characterize the isolated chitin. Chitinous waste degradation was studied in terms of chitinase production.

Endochitinase와 Chitobiosidase 유전자의 동시발현에 의한 키틴분해 활성의 증가 (Enhancement of chitinolytic activity of by co-expression of endochitinase and chitobiosidase genes)

  • 김정태;최신건
    • 산업기술연구
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    • 제30권B호
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    • pp.69-74
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    • 2010
  • Chitinolytic activity was enhanced by coexpression of endo-chitinase gene (chiA) and chitobiosidase gene (chiB) from Serratia marcescens KFRI314 using constitutive expression vector, pHCEIA, in E. coli. Coexpression vector was constructed by inserting ribosome binding site (RBS) into junction between two chitinase genes. SDS-PAGE analyses showed that two chitinase were constitutively expressed while E. coli clones expressing two chitinases simultaneously increased halo size on colloidal chitin plate. Furthermore, the chitinolytic activities were much enhanced in coexpressed clones when degradation patterns of substrate analogues such as 4-MU-(NAG), $4-MU-(NAG)_2$,$4-MU-(NAG)_3$ were used. Consequently, the combined use of endochitinase and chitobiosidase greatly increased overall chitinolytic activities on recombinant E. coli clones.

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The Degradation of Chitin with Food Grade Papain

  • Han, Beom-Ku;You, Tak;Moon, Jong-Kook;Kim, Sae-Bom;Jo, Do-Hyun
    • Journal of Applied Biological Chemistry
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    • 제43권4호
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    • pp.246-249
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    • 2000
  • We investigated the production of chitin oligosaccharides using food grade papain. A solution of commercial food grade papain (FGP) was dialyzed for 12 h before measuring its chitinolytic activity. The effects of enzyme concentration, reaction temperature, and pH on the endochitinase and $\beta$-N-acetylglucosaminidase activities and the thermostability of these enzymes were investigated. In adddition, the reaction products were analyzed with gel filtration on a Bio-Gel P2. The endochitinase activity was twentyfold higher than that of $\beta$-N-acetylglucosaminidase. The optimal endochitinase activity was at pH 3.0, while the maximal $\beta$-N-acetylglucosaminidase activity was at pH 6.0. The reaction product consisted mainly of the dimer of N -acetylglucosamine, with a small amount of its trimer. Under the experimental conditions, $120{\mu}g$ of chitin oligomers were obtained with 1 mg of FGP protein after an incubation of 2 h.

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Chitinase를 생성하는 Serratia sp. JM의 분리 및 특성 (Isolation and Characterization of Serratia sp. JM Producing Chitinase)

  • 차진명;진상기고한철이인화
    • KSBB Journal
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    • 제11권1호
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    • pp.92-98
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    • 1996
  • 전남 법성포 해안의 갯벌 시료로부터 chitinase 생 생 균주를 분리하였으며, 분리된 균주 중에서 chiti­n nase 생성능이 우수한 JM을 선발 동정하여 Serranasetia sp. JM으로 명명하였다. Serratia sp. JM은 nu­trient 배지냐 MacConkey 배지에서 prodigiosin 색소를 생성하며, 정제 chitin이 포함된 한천 배지에서 는 chitinase 생성에 따른 clear zone 형성이 확인되 었다 Serratia sp. JM은 형태적, 생리.생화학적 특 성과 유기물 동화는 SUCCIniC, urea 및 pyruvic 산 을 제외하고는 공시 균주인 Serratia marcescens ATCC 27117과 유사하였으며, tetracyclin에 대해 서는 항생제에 대한 내성을 가지고 있었으나, kanamycin과 chloramphenicol에 대해서는 내성을 가지지 않았다. Serratia sp. JM의 chitinase 생성에 따른 최적온도와 pH는 $30^{\circ}C$ 와 7.5로 냐타났다. Serratia sp. JM은 120시간까지는 배양 시간이 증가 함에 따라 chiti-nase 생성과 pH는 점차 증가하였으 나, 배양 120시간 이후에는 chitin 분해에 따른 acetic acid의 축적에 따라 chitinase 생성과 pH는 감소 하였다.

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Correlation between pr1 and pr2 Gene Content and Virulence in Metarhizium anisopliae Strains

  • Rosas-Garcia, Ninfa M.;Avalos-de-Leon, Osvaldo;Villegas-Mendoza, Jesus M.;Mireles-Martinez, Maribel;Barboza-Corona, J.E.;Castaneda-Ramirez, J.C.
    • Journal of Microbiology and Biotechnology
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    • 제24권11호
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    • pp.1495-1502
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    • 2014
  • Metarhizium anisopliae is a widely studied model to understand the virulence factors that participate in pathogenicity. Proteases such as subtilisin-like enzymes (Pr1) and trypsin-like enzymes (Pr2) are considered important factors for insect cuticle degradation. In four M. anisopliae strains (798, 6342, 6345, and 6347), the presence of pr1 and pr2 genes, as well as the enzymatic activity of these genes, was correlated with their virulence against two different insect pests. The 11 pr1 genes (A, B, C, D, E, F, G, H, I, J, and K) and pr2 gene were found in all strains. The activity of individual Pr1 and Pr2 proteases exhibited variation in time (24, 48, 72, and 96 h) and in the presence or absence of chitin as the inductor. The highest Pr1 enzymatic activity was shown by strain 798 at 48 h with chitin. The highest Pr2 enzymatic activity was exhibited by the 6342 and 6347 strains, both grown with chitin at 24 and 48 h, respectively. Highest mortality on S. exigua was caused by strain 6342 at 48 h, and strains 6342, 6345, and 6347 caused the highest mortality 7 days later. Mortality on Prosapia reached 30% without variation. The presence of subtilisin and trypsin genes and the activity of these proteases in M. anisopliae strains cannot be associated with the virulence against the two insect pests. Probably, subtilisin and trypsin enzyme production is not a vital factor for pathogenicity, but its contribution is important to the pathogenicity process.