Hyperproduction and application of α-agarase to enzymatic enhancement of antioxidant activity of porphyran
Hyperproduction and application of α-agarase to enzymatic enhancement of antioxidant activity of porphyran
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DOI：
10.1021/jf0613684
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发表时间：
2006-12-27
影响因子：
6.1
通讯作者：
Horikoshi, Koki
中科院分区：
文献类型：
--
作者：
Hatada, Yuji;Ohta, Yukari;Horikoshi, Koki
报道了地中海单胞菌α-琼脂糖苷酶基因AgaA33的核苷酸序列。对菌株JAMB-A33进行了鉴定。AGaA33的开放阅读框编码1463个氨基酸残基。我们以枯草芽孢杆菌为宿主，成功地在胞外高效生产重组α-琼脂酶(AgaA33)。这是重组生产α-琼脂酶的首次报道。此外，我们还证明了α-琼脂酶对紫菜多糖中的α-1，3键的水解是提高其清除自由基能力和清除超氧阴离子能力的重要步骤，而β-琼脂酶对紫菜多糖中的β-1，4键的水解并不能显著提高其抗氧化活性。
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 alpha-agarase (AgaA33) efficiently using Bacillus subtilis as a host. This is the first report of recombinant production of alpha-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.