Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21

Jiang Li; Yujie Sha

doi:10.1007/s00343-015-4072-3

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Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21

Updated：2023-05-16

- Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21
- Journal of Oceanology and Limnology Vol. 33, Issue 2, Pages: 319-327(2015)
- Affiliations：
  
  1. Key Lab of Marine Bioactive Substances First Institute of Oceanography State Oceanic Administration (SOA)
  2. Institute of Oceanology Chinese Academy of Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-015-4072-3
  CLC：
- Online First：06 November 2014，
  
  Published：2015
- Accepted：
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Li, J., Sha, Y. Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21., Chin. J. Ocean. Limnol. 33, 319–327 (2015). https://doi.org/10.1007/s00343-015-4072-3
DOI：

Li, J., Sha, Y. Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21., Chin. J. Ocean. Limnol. 33, 319–327 (2015). https://doi.org/10.1007/s00343-015-4072-3 DOI：

摘要

Abstract

An agar-degrading bacterium

designated as Pseudoalteromonas sp. NJ21

was isolated from an Antarctic sediment sample. The agarase gene aga1161 from Pseudoalteromonas sp. NJ21 consisting of a 2 382-bp coding region was cloned. The gene encodes a 793-amino acids protein and was found to possess characteristic features of the Glyco_hydro_42 family. The recombinant agarase (rAga1161) was overexpressed in Escherichia coli and purified as a fusion protein. Enzyme activity analysis revealed that the optimum temperature and pH for the purified recombinant agarase were 30–40°C and 8.0

respectively. rAga1161 was found to maintain as much as 80% of its maximum activity at 10°C

which is typical of a coldadapted enzyme. The pattern of agar hydrolysis demonstrated that the enzyme is an β-agarase

producing neoagarobiose (NA2) as the final main product. Furthermore

this work is the first proof of an agarolytic activity in Antarctic bacteria and these results indicate the potential for the Antarctic agarase as a catalyst in medicine

food and cosmetic industries.

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