• 생명과학회지
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• 제9권4호
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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.

• Journal of Microbiology and Biotechnology
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• 제34권1호
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• pp.132-140
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• 2024

In this study, carrageenase immobilization was evaluated with a concise and efficient strategy. Pomelo peel cellulose (PPC) modified by polyethyleneimine (PEI) using the physical absorption method was used as a carrier to immobilize carrageenase and achieved repeated batch catalysis. In addition, various immobilization and reaction parameters were scrutinized to enhance the immobilization efficiency. Under the optimized conditions, the enzyme activity recovery rate was more than 50% and 4.1 times higher than immobilization with non-modified pomelo peels. The optimum temperature and pH of carrageenase after immobilization by PEI-modified pomelo peel, at 60℃ and 7.5 respectively, were in line with the free enzyme. The temperature resistance was reduced, inconsistent with free enzyme, and pH resistance was increased. A significant loss of activity (46.8%) was observed after reusing it thrice under optimal reaction conditions. In terms of stability, the immobilized enzyme conserved 76.0% of the initial enzyme activity after 98 days of storage. Furthermore, a modest decrease in the kinetic constant (K_m) value was observed, indicating the improved substrate affinity of the immobilized enzyme. Therefore, modified pomelo peel is a verified and promising enzyme immobilization system for the synthesis of inorganic solvents.

• 생명과학회지
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• 제9권4호
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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.

• Journal of Microbiology and Biotechnology
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• 제26권2호
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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 K_m and V_max 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.

• Fisheries and Aquatic Sciences
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• 제9권2호
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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.

• 한국수산학회:학술대회논문집
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• 한국수산학회 2005년도 춘계학술대회
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• pp.67-68
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• 2005

• 한국양식학회:학술대회논문집
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• 한국양식학회 2004년도 수산관련학회 공동학술대회 발표요지집
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• pp.142-143
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• 2004

• 미생물학회지
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• 제54권3호
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• pp.299-301
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• 2018

Microbulbifer agarilyticus GP101은 소라(Turbo cornutus)의 내장에서 분리되었으며 해조류 유래 다당류인 한천, 알긴산, ${\kappa}$-카라기난을 분해하는 특징이 있다. GP101 균주의 유전체는 4,255,625 bp 크기로 3,458개의 코딩 서열을 포함하며 55.4%의 GC 함량을 가진다. BLASTP 분석 결과 7개의 agarase, 5개의 alginate lyase, 10개의 glucanase, 4개의 chitinase, 2개의 xylanases, 1개의 ${\kappa}$-carrageenase, 1개의 laminarinase의 존재를 확인하였다. M. agarilyticus GP101의 유전체 정보는 다당류의 생물전환 공정에 이용할 수 있는 유전 정보를 제공할 수 있을 것이다.

• 미생물학회지
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• 제54권4호
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• pp.463-464
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• 2018

Tamlana sp. UJ94는 해수로부터 분리되었으며 알긴산을 분해할 수 있다. 알긴산 분해 관련 특성을 이해하기 위해 이 세균의 유전체를 분석하였다. UJ94의 유전체는 4,116,543 bp의크기로 3,609개의 코딩서열을 가지고 있으며 35.2 mol%의 G + C 함량을 가진다. BLASTp 검색 결과 9개의 alginate lyase 외에도 6개의 agarase, 5개의 amylase, 4개의 carrageenase, 1개의 cellulase, 4개의 pectate lyase, 7개의 xylanase의 존재가 예측되어 UJ94의 다양한 다당류 분해 능력을 암시하였다. Tamlana sp. UJ94의 유전체는 생물전환 공정에 사용할 수 있는 다당류 분해 유전자를 제공할 수 있을 것이다.