| 海洋细菌QY202产κ-卡拉胶酶的分离纯化和性质研究 |
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| 引用本文： | 段高飞,苏贝,韩峰,于文功.海洋细菌QY202产κ-卡拉胶酶的分离纯化和性质研究[J].中国海洋大学学报(自然科学版),2010,40(3). |
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| 作者姓名： | 段高飞 苏贝 韩峰 于文功 |
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| 作者单位： | 中国海洋大学医药学院,山东,青岛,266003 |
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| 基金项目： | 国家高技术研究发展计划项目，青岛市科技攻关项目 |
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| 摘 要： | 为获得高效降解卡拉胶菌株,从青岛太平角海域采集的角叉菜表面分离到1株高产κ-卡拉胶酶的海洋交替假单胞菌(Pseudoalteromonas sp.)QY202,经硫酸铵沉淀、脱盐、DEAE阴离子交换层析等步骤从该菌株发酵液上清中分离纯化得到1种专一性降解κ-卡拉胶的κ-卡拉胶酶,并研究了该酶的基本酶学性质.结果表明该酶被纯化了23.1倍,回收率为43.9%,分子量大小为33.2 kDa.酶的最适反应温度为40 ℃,最适反应pH为8.0,在0～40 ℃,pH=7.0～8.0之间酶活力较稳定.酶对底物κ-卡拉胶的米氏常数Km值为1.6 mg/mL.Na~+、K~+对酶活有促进作用,而Hg~(2+)、Cu~(2+)强烈抑制酶的活性.酶解κ-卡拉胶的主产物为硫酸新κ-卡拉二糖和硫酸新κ-卡拉四糖.
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| 关 键 词： | κ-卡拉胶酶 交替假单胞菌 分离纯化 性质研究 κ-carrageenase |
Purification and Characterization of a κ-carrageenase from Marine Pseudoalteromonas sp. QY202 |
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| DUAN Gao-Fei,SU Bei,HAN Feng,YU Wen-Gong.Purification and Characterization of a κ-carrageenase from Marine Pseudoalteromonas sp. QY202[J].Periodical of Ocean University of China,2010,40(3). |
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| Authors: | DUAN Gao-Fei SU Bei HAN Feng YU Wen-Gong |
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| Institution: | DUAN+Gao-Fei,SU+Bei,HAN+Feng,YU+Wen-Gong(School+of+Medicine+,+Pharmacy,Ocean+University+of+China,Qingdao+266003,China) |
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| Abstract: | A marine bacterium Pseudoalteromonas sp. QY202 with high κ-carrageenase activity was isolated from the surface of Chondrus crispus. The κ-carrageenase was purified to electrophoretic homogeneity from the culture supernatant by a procedure of ammonium sulfate precipitation, desalting and DEAE-sepharose ion exchange chromatography, and the characterization of the enzyme was studied. The results show that the enzyme is purified 23.1 folds with a total recovery yield of 43.9% and gives a single band on SDS-PAGE with a molecular mass of 33.2 kDa. The optimum temperature and pH for enzyme activity are 40 ℃ and pH8.0, respectively. The enzyme is stable at temperatures below 40 ℃ and over a range of pH7.0～8.0. For κ-carrageenan, the enzyme gave a Km value of 1.6 mg/mL. The enzyme activity could be enhanced by the presence of Na~+ and K~+, whereas enormously inhibited by Hg~(2+)and Cu~(2+). The main hydrolysis products of κ-carrageenan by the enzyme are κ-neocarradiaose and κ- neocarratetraose. |
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| Keywords: | Pseudoaltermonas purification characterization |
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