Hyperproduction and application of alpha-agarase to enzymatic enhancement of antioxidant activity of porphyran.
The nucleotide sequence of the gene for the alpha-agarase, AgaA33, from Thalassomonas sp. strain JAMB-A33 was determined. The open reading frame for AgaA33 was revealed to encode 1463 amino acid residues. We succeeded in extracellular production of recombinant -agarase (AgaA33) efficiently using Bacillus subtilis as a host. This is the first report of recombinant production of -agarase. Furthermore, we demonstrated that hydrolysis of alpha-1,3 linkages in porphyran, a sulfated polysaccharide from marine red algae, by alpha-agarase is an important step for improvement of its antioxidant activity with regard to free-radical-scavenging capacity and superoxide radical anion scavenging activity, whereas the hydrolysis of beta-1,4 linkages in porphyran by beta-agarase did not increase on the antioxidant activity markedly.
Hatada
Yuji
Y
Japan Agency for Marine-Earth Science and Technology, 2-15 Natsushima, Yokosuka 237-0061, Japan. hataday@jamstec.go.jp
Ohta
Yukari
Y
Horikoshi
Koki
K
D000595:Amino Acid Sequence; D000975:Antioxidants / Q000378:metabolism / Q000494:pharmacology*; D001483:Base Sequence; D002236:Carbohydrate Conformation; D004269:DNA, Bacterial / Q000737:chemistry; D020563:Gammaproteobacteria / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011994:Recombinant Proteins / Q000378:metabolism; D000461:Rhodophyta / Q000737:chemistry; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology
D000975:Antioxidants; D004269:DNA, Bacterial; D011994:Recombinant Proteins; C038549:porphyran; D012685:Sepharose; D006026:Glycoside Hydrolases; C019624:agarase