• Title/Summary/Keyword: Carrageenase

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Purification and Characterization of Carrageenase from Pseudomonas alcaligenes JCL-43 (Pseudomonas alcaligenes JCL-43이 생산하는 Carrageenase의 정제 및 특성)

  • 주동식;조순영;이정석;이응호;양승택
    • Journal of Life Science
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    • v.9 no.4
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    • pp.414-422
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    • 1999
  • Our works performed for preparation of oligosaccharides from carrageenan, seaweed polysaccharide, and one active strain for carrageenan was isolated from sea water and identified to Pseudomonas alcaligenes. Carrageenan degrading enzyme was purified from the culture fluid of isolated strain-Pseudomonas alcaligenes JCL-43, by DEAE-Cellulose, Sephadex G-100, Q-Sepharose and CM Sepharose CL-6B column chromatography. Two enzyme-F-I, F-II- was identified this purifying process, and the molecular weight of the purified carrageenase were estimated to be 23.6kDa and 30.2kDa, respectively. The optimum pH and temperature for two carrageenase activity were 7.0 and 4$0^{\circ}C$. These enzymes were stable in the pH range of 6.0~7.5 and lower than 5$0^{\circ}C$, and required 1.5% NaCl for optimum activity. And these carragennase were inhibited by metal ions such as Cu2+, Zn2+, Hg2+, but increased by Ba2+ and Ca2+, and showed specificity on -carrageenan.

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Preparation of Carrageenan Oligosaccharides Using Carrageenase from Pseudomonas alcaligenes JCL-43 and Its Functional Properties (Pseudomonas alcaligenes JCL-43 유래 Carrageenase를 이용한 카라기난 올리고당의 제조 및 기능 특성)

  • 주동식;조순영;이응호;양승택
    • Journal of Life Science
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    • v.9 no.4
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    • pp.423-429
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    • 1999
  • Carrageenan oligosaccharides prepared from -carrageenan by carrageenase from Pseudomonas alcaligenes. The oligosaccharides showed three spots on TLC and the degree of Polymerization of the C1, C2 and C3 spot were each 9.0$\pm$1.0, 6.0$\pm$1.5 and 2.5$\pm$1.5, respectively. Each hydrolysates and spots-C1, C2, C3-were tested the several functionalities such as antimicrobial activity, anticavity activity and anticoagulant activity. The antimicrobial and anticavity activity of carrageenan hydrolysates and oligosaccharide fractions were very low, but the anticoagulant activity was identified in all samples.

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Purification and Characterization of a New κ-Carrageenase from the Marine Bacterium Vibrio sp. NJ-2

  • Zhu, Benwei;Ning, Limin
    • Journal of Microbiology and Biotechnology
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    • v.26 no.2
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    • pp.255-262
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    • 2016
  • The carrageenan-degrading marine bacterium Vibrio sp. strain NJ-2 was isolated from rotten red algae, and κ-carrageenase with high activity was purified from the culture supernatant. The purified enzyme with molecular mass of 33 kDa showed the maximal activity of 937 U/mg at 40℃ and pH 8.0. It maintained 80% of total activity below 40℃ and between pH 6.0 and 10.0. The kinetics experiment showed the Km and Vmax values were 2.54 g/ml and 138.89 mmol/min/mg, respectively. The thin layer chromatography and ESI-MS analysis of hydrolysates indicated that the enzyme can endolytically depolymerize the κ-carrageenan into oligosaccharides with degrees of depolymerization of 2-8. Owing to its high activity, it could be a valuable tool to produce κ-carrageenan oligosaccharides with various biological activities.

Optimal Culture Conditions and Isolation of a ι-Carrageenase-producing Marine Bacterium

  • Shim Hang-Sun;Lim Su-Jin;Choi Min-Jung;Kim Jong-Oh;Kim Seok-Ryel;Kim Hyeung-Rak
    • Fisheries and Aquatic Sciences
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    • v.9 no.2
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    • pp.57-63
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    • 2006
  • A bacterial strain capable of hydrolyzing carrageenan was isolated from the coast of Busan in Korea. The isolated strain (HS5322) is aerobic, gram-negative, rod-shaped, and motile. Comparison of the 16S rDNA of the isolate with that of known Pseudomonas sp. showed that sequence similarity was at most 95%, implying that the isolate is a new Pseudomonas species. The organism grew optimally at NaCl concentrations of 2.0 to 2.5%. The optimum temperature and pH for carrageenase production in a 72-h flask culture containing 1% carrageenan was $20^{\circ}C$ and pH 8.5, respectively. Of the synthetic substrates tested, the highest enzyme activity was obtained with p-nitrophenyl ${\beta}$-D-galactopyranoside.

Complete genome sequence of Microbulbifer agarilyticus GP101 possessing genes coding for diverse polysaccharide-degrading enzymes (다양한 다당류를 분해하는 세균 Microbulbifer agarilyticus GP101의 완전한 유전체 서열)

  • Jung, Jaejoon;Bae, Seung Seob;Chung, Dawoon;Baek, Kyunghwa
    • Korean Journal of Microbiology
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    • v.54 no.3
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    • pp.299-301
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    • 2018
  • Microbulbifer agarilyticus GP101 was isolated from the gut of a marine invertebrate Turbo cornutus and capable of degrading polysaccharide such as agar, alginate, and ${\kappa}$-carrageenan constituting algal cell wall. To obtain genomic basis of polysaccharide-degrading activity, we sequenced genome of strain GP101. The genome consists of 4,255,625 bp, 3,458 coding sequences with 55.4% G + C contents. BLASTP search revealed the presence of seven agarases, five alginate lyases, ten glucanases, four chitinases, two xylanases, one ${\kappa}$-carrageenase, and one laminarinase. The genomic data of strain GP101 will provide potential uses in the bioconversion process of diverse polysaccharide into bioenergy and biochemicals.

Complete genome sequence of Tamlana sp. UJ94 degrading alginate (알긴산을 분해하는 세균 Tamlana sp. UJ94의 완전한 유전체 서열)

  • Jung, Jaejoon;Bae, Seung Seob;Chung, Dawoon;Baek, Kyunghwa
    • Korean Journal of Microbiology
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    • v.54 no.4
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    • pp.463-464
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    • 2018
  • Tamlana sp. UJ94 isolated from seawater can degrade alginate. To identify the genomic basis of this activity, the genome was sequenced. The genome was composed of 4,116,543 bp, 3,609 coding sequences, and 35.2 mol% G + C content. A BLASTp search predicted the presence of 9 alginate lyases as well as 6 agarases, 5 amylases, 4 carrageenases, 1 cellulase, 4 pectate lyases, and 7 xylanases, indicating its ability to degrade diverse polysaccharides. The genome of strain UJ94 is a source of polysaccharide-degrading enzymes for bioconversion processes.