Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica

Jihong Shen; Guangfeng Kan; Cuijuan Shi; Zhenhuan Lei; Qiuju Xie; Wenjia Qian

doi:10.1007/s00343-011-0311-4

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Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica

Updated：2023-05-16

- Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica
- Journal of Oceanology and Limnology Vol. 29, Issue 5, Pages: 1086-1092(2011)
- Affiliations：
  
  1. Key Laboratory of Marine Bio-active Substances State Oceanic Administration
  2. School of the Ocean Harbin Institute of Technology at Weihai
- Author bio：
- Funds：
- DOI：10.1007/s00343-011-0311-4
  CLC：
- Online First：08 August 2011，
  
  Published：2011
- Accepted：
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Shen, J., Kan, G., Shi, C. et al. Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica., Chin. J. Ocean. Limnol. 29, 1086–1092 (2011). https://doi.org/10.1007/s00343-011-0311-4
DOI：

Shen, J., Kan, G., Shi, C. et al. Purification and characterization of cold-active endo-1,4-β-glucanase produced by Pseudoalteromonas sp. AN545 from Antarctica., Chin. J. Ocean. Limnol. 29, 1086–1092 (2011). https://doi.org/10.1007/s00343-011-0311-4 DOI：

摘要

Abstract

A bacterium hydrolyzing carboxymethylcellulose

isolated from Antarctic sea ice

was identified as Pseudoalteromonas sp. based on 16S rDNA gene sequences and named as Pseudoalteromonas sp. AN545. The extracellular endo-1

4-β-glucanase AN-1 was purified successively by ammonium sulfate precipitation

DEAE-Sepharose ion exchange chromatography and Sephadex G-75 gel filtration chromatography. The molecular mass of AN-1 was estimated to be 47.5 kDa utilizing SDS-PAGE and gel chromatography analysis. AN-1 could hydrolyze caboxymethylcellulose

avicel and β-glucan

but not cellobiose

xylan and p-Nitrophenyl-β-D-glucopyranoside. The optimal temperature and pH for the β-glucanase activity of AN-1 were determined to be at 30°C and pH 6.0

respectively. AN-1 was stable at acidic solutions of pH 5.0–6.5 and temperatures below 30°C for 1 h. Moreover

the specific activity was enhanced by Ca2+ and Mg2+

and inhibited by Cu2+. The kinetic parameters Michaelis constant (K m) and maximum velocity (V max) of AN-1 were 3.96 mg/mL and 6.06×10−2 mg/(min·mL)

respectively.

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references

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