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    • 10. 发明申请
    • HYBRID ALPHA-AMYLASES
    • 混合阿尔法胺
    • US20120021485A1
    • 2012-01-26
    • US13132881
    • 2009-12-11
    • Scott D. PowerAndrew Shaw
    • Scott D. PowerAndrew Shaw
    • C12N9/96G06G7/60C12N1/21C12N1/15C12N15/62C12N15/63
    • C12N9/2417C07K2319/00G06F19/12G06F19/16
    • Hybrid alpha-amylases are provided that share a conserved 3D structure in whole or in part with a wild-type Termamyl-like ?-amylase, e.g., a Bacillus amylase. In the hybrid, an N terminal portion of a Termamyl-like ?-amylase is replaced with sequences from an archae ? amylase. The sequence similarity between the two amylase sequences may be less than 60%. Conserving the wild-type 3D structure in the hybrid facilitates obtaining enzymatically active amylases. In one embodiment, one or both amylase sequences contribute residues to the B domain, resulting in particularly advantageous properties. For instance, replacement of the Ca2+ binding site in the B domain of the Termamyl-like ?-amylase with a B domain sequence of an archae ? amylase that does not bind Ca2+ can produce a hybrid that is fully active in the absence of Ca2+.
    • 提供杂交α-淀粉酶,其与野生型类戊酰样α-淀粉酶(例如芽孢杆菌淀粉酶)全部或部分共享保守的3D结构。 在杂交体中,类戊酰样α-淀粉酶的N末端部分被来自古细菌的序列替代 淀粉酶。 两个淀粉酶序列之间的序列相似性可以小于60%。 在杂交中保护野生型3D结构有助于获得酶活性淀粉酶。 在一个实施方案中,一个或两个淀粉酶序列向B结构域贡献残基,导致特别有利的性质。 例如,用具有古细菌的B结构域序列的Termamyl样α-淀粉酶的B结构域中的Ca 2+结合位点的替换 不结合Ca2 +的淀粉酶可以产生在不存在Ca 2+的情况下完全活性的杂交体。