Purification and Characterization of a New Thermostable κ-CarrageenasefromtheMarineBacterium Pseudoalteromonas sp. QY203  

作　　者：LI Shangyong JIA Panpan WANG Linna YU Wengong HAN Feng 

机构地区：[1]Key Laboratory of Marine Drugs, Chinese Ministry of Education [2]Provincial Key Laboratory of Glycoscience and Glycotechnology of Shandong Province and School of Medicine and Pharmacy, Ocean University of China

出　　处：《Journal of Ocean University of China》2013年第1期155-159,共5页中国海洋大学学报（英文版）

基　　金：supported by National Science Foundation of China (31000361 and 31070712);Program for Changjiang Scholars and Innovative Research Team in University (IRT0944);Special Fund for Marine Scientific Research in the Public Interest (201005024);the Fundamental Research Funds for the Central Universities(201013008)

摘　　要：A new extracellular κ-carrageenase, namely CgkP, 34.0 kDa in molecular weight, was purified from Pseudoalteromonas sp. QY203. CgkP showed relatively high activity at acidities ranging from pH6.0 to pH9.0 and temperatures ranging from 30℃ to 50℃ with the highest activity at 45℃ and pH7.2. Sodium chloride increased its activity markedly, and KC1 increased its activity slightly. The divalent and trivalent metal ions including Cu^2＋, Ni^2＋, Zn^2＋, Mn^2＋, Al^3＋ and Fe^3＋ significantly inhibited its activity, while Mg^2＋ did not. CgkP remained 70% of original activity after being incubated at 40℃ for 48h, and remained 80% of the activity after being incubated at 45℃ for 1 h. It exhibited endo-κ-carrageenase activity, mainly depolymerizing the κ-carrageenan into disaccharide and tetrasaccharide. CgkP was more thermostable than most of previously reported κ-carrageenases with a potential of being used in industry.A new extracellular κ-carrageenase, namely CgkP, 34.0 kDa in molecular weight, was purified from Pseudoalteromonas sp. QY203. CgkP showed relatively high activity at acidities ranging from pH6.0 to pH9.0 and temperatures ranging from 30℃ to 50℃ with the highest activity at 45℃ and pH7.2. Sodium chloride increased its activity markedly, and KCl increased its activity slightly. The divalent and trivalent metal ions including Cu2+ , Ni2+ , Zn2+ , Mn2+ , Al3+ and Fe3+ significantly inhibited its activity, while Mg2+ did not. CgkP remained 70% of original activity after being incubated at 40℃ for 48 h, and remained 80% of the activity after being incubated at 45℃ for 1 h. It exhibited endo-κ-carrageenase activity, mainly depolymerizing the κ-carrageenan into disaccharide and tetrasaccharide. CgkP was more thermostable than most of previously reported κ-carrageenases with a potential of being used in industry.

关 键 词：κ-carrageenase PURIFICATION CHARACTERIZATION thermostability PSEUDOALTEROMONAS 

分 类 号：Q946[生物学—植物学]