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KMID : 1007520150240051811
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Food Science and Biotechnology
2015 Volume.24 No. 5 p.1811 ~ p.1816
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Affinity Purification of 4-α-Glucanotransferase through Formation of Complex with Insoluble Amylose
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Yoon Sun-Hee
Kim Min-Su
Kim Yong-Ro
Kim Young-Wan
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Abstract
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4-α-Glucanotransferases (αGTases) are useful enzymes to modify starch structure using their unique hydrolysis pattern and transglycosylation activity. In spite of lacking of a carbohydrate binding module, a thermostable αGTase from Thermus thermophilus (TTαGT) bound to insoluble amylose, leading to simple recovery of the enzyme-amylose complex using centrifugation. At a preparative scale, the recovery yield was 40.3% of the subjected free enzyme via collection of the complex twice. The complex exhibited improved thermostability, which shifted the optimum temperature from 70 to 80°C and increased the half-life at 90°C by three-fold compared with the free enzyme. Texture profile analysis of the gels made of modified starch by either free TTαGT or the complex revealed that the complex with double dosage showed the performance similar to free TTαGT in the modification of starch. In conclusion, the purification method described here would be useful due to easy scale-up and simple process without chromatographic process.
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KEYWORD
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4-α-glucanotransferase, affinity purification, amylose, thermostabilization, starch modification
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