16033-31-1Relevant articles and documents
Overexpression and characterization of a novel thermostable β-agarase YM01-3, from marine bacterium Catenovulum agarivorans YM01T
Cui, Fangyuan,Dong, Sujie,Shi, Xiaochong,Zhao, Xia,Zhang, Xiao-Hua
, p. 2731 - 2747 (2014/06/10)
Genome sequencing of Catenovulum agarivorans YM01T reveals 15 open-reading frames (ORFs) encoding various agarases. In this study, extracellular proteins of YM01T were precipitated by ammonium sulfate and separated by one-dimensional gel electrophoresis. The results of in-gel agarase activity assay and mass spectrometry analysis revealed that the protein, YM01-3, was an agarase with the most evident agarolytic activity. Agarase YM01-3, encoded by the YM01-3 gene, consisted of 420 amino acids with a calculated molecular mass of 46.9 kDa and contained a glycoside hydrolase family 16 β-agarase module followed by a RICIN superfamily in the C-terminal region. The YM01-3 gene was cloned and expressed in Escherichia coli. The recombinant agarase, YM01-3, showed optimum activity at pH 6.0 and 60°C and had a Km of 3.78 mg mL-1 for agarose and a Vmax of 1.14 × 104 U mg-1. YM01-3 hydrolyzed the β-1,4-glycosidic linkages of agarose, yielding neoagarotetraose and neoagarohexaose as the main products. Notably, YM01-3 was stable below 50°C and retained 13% activity after incubation at 80°C for 1 h, characteristics much different from other agarases. The present study highlights a thermostable agarase with great potential application value in industrial production.
13C-N.M.R.-SPECTROSCOPIC INVESTIGATION OF AGAROSE OLIGOMRS
Rochas, Cyrille,Lahaye, Marc,Yaphe, Wilfred,Viet, Minh Tan Phan
, p. 199 - 208 (2007/10/02)
A complete, unambiguous assignment of all of the 13C-n.m.r.-spectral signals of agarose oligomers produced by enzymic hydrolysis has been achieved.The 1J 13C-H coupling constants are reported, and the chemical shifts and coupling constants of both the agarose polymer and oligomers are compared.
