Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium <i>Pseudoalteromonas</i> sp. NJ21 -- Journal of Oceanology and Limnology,2015,33(2):319-327

	Cite this paper:
	LI Jiang, SHA Yujie. Expression and enzymatic characterization of a cold-adapted β-agarase from Antarctic bacterium Pseudoalteromonas sp. NJ21[J]. Journal of Oceanology and Limnology, 2015, 33(2): 319-327

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

LI Jiang¹, SHA Yujie²

1 Key Lab of Marine Bioactive Substances, First Institute of Oceanography, State Oceanic Administration (SOA), Qingdao 266061, China;
2 Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China

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 purifi ed as a fusion protein. Enzyme activity analysis revealed that the optimum temperature and pH for the purifi ed recombinant agarase were 30-40℃ and 8.0, respectively. rAga1161 was found to maintain as much as 80% of its maximum activity at 10℃, 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 fi nal 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.

Key words: Antarctic bacterium Pseudoalteromonas|agarase|expression|enzymatic characterization

Received: 2014-03-20 Revised: 2014-06-02

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