Modification of the transglucosylation properties of α-glucosidases from Aspergillus oryzae and Aspergillus sojae via a single critical amino acid replacement
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Abstract We constructed enzyme variants of the α-glucosidases from Aspergillus oryzae (AoryAgdS) and Aspergillus sojae (AsojAgdL) by mutating the amino acid residue at position 450. AoryAgdS_H450R acquired the ability to produce considerable amounts of α-1,6-transglucosylation products, whereas AsojAgdL_R450H changed to produce more α-1,3- and α-1,4-transglucosylation products than α-1,6-products. The 450th amino acid residue is critical for the transglucosylation of these α-glucosidases.
2014 ◽
Vol 52
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pp. 11-19
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2018 ◽
Vol 102
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pp. 6537-6545
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1997 ◽
Vol 78
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pp. 1419-1420
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1974 ◽
Vol 39
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pp. 1290-1302
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1987 ◽
Vol 262
(8)
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pp. 3754-3761
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