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KMID : 0545120110210111116
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Journal of Microbiology and Biotechnology
2011 Volume.21 No. 11 p.1116 ~ p.1122
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Improvement in the Catalytic Activity of β-Agarase AgaA from Zobellia galactanivorans by Site-Directed Mutagenesis
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Lee Seung-Woo
Lee Dong-Geun
Jang Min-Kyung
Jeon Myong-Je
Jang Hye-Ji
Lee Sang-Hyeon
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Abstract
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In this study, site-directed mutagenesis was performed on the β-agarase AgaA gene from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutant enzymes, S63K, C253I, and S63K-C253I, were 126% (1,757.78 U/mg), 2.4% (33.47 U/mg), and 0.57% (8.01 U/mg), respectively, relative to the wildtype β-agarase AgaA (1,392.61 U/mg) at 40oC. The stability of the mutant S63K enzyme was 125% of the wild-type up to 45oC, where agar is in a sol state. The mutant S63K enzyme produced 166%, 257%, and 220% more neoagarohexaose, and 230%, 427%, and 350% more neoagarotetraose than the wild-type in sol, gel, and nonmelted powder agar, respectively, at 45oC over 24 h. The mutant S63K enzyme produced 50% more neoagarooligosaccharides from agar than the wild-type β-agarase AgaA from agarose under the same conditions. Thus, mutant S63K β-agarase AgaA may be useful for the production of functional neoagarooligosaccharides.
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KEYWORD
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β-agarase AgaA, activity improvement, site-directed mutagenesis, Zobellia galactanivorans
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