PHYTASE MUTANT
    1.
    发明申请

    公开(公告)号:US20210207112A1

    公开(公告)日:2021-07-08

    申请号:US17059696

    申请日:2019-05-30

    发明人: Aixi Bai Feng Li

    IPC分类号: C12N9/16

    摘要: Disclosed is a thermostable phytase, in which at least one pair of introduced disulfide bonds is included in the amino acid sequence of wild-type Escherichia coli phytase or mutant Escherichia coli phytase, and after the introduction, the properties of the phytase can be improved, especially the heat stability, steam stability and granulation stability, which are superior to those of the existing wild-type or mutant phytase; compared to the engineered phytase in which disulfide bonds are introduced, the heat stability is also significantly improved.

    L-TYPE AMYLASE VARIANT AND USE THEREOF
    4.
    发明申请

    公开(公告)号:US20180340161A1

    公开(公告)日:2018-11-29

    申请号:US15989534

    申请日:2018-05-25

    发明人: Yan Fan Yan Sun Hong Xu

    IPC分类号: C12N9/28

    摘要: The present invention discloses an L-type amylase variant and use thereof. The α-amylase variant is obtained by deleting the first N-terminal amino acid residue V from the α-amylase of B. licheniformis and replacing it with three other amino acid residues DGL. The α-amylase variant provided by the present invention has high catalytic activity under the acidic conditions of pH 5.0-5.8 and a high temperature of 100° C. or above. The acid resistance and thermal stability of these α-amylase variants are suitable for starch liquefaction.

    L-type amylase variant and use thereof

    公开(公告)号:US10647970B2

    公开(公告)日:2020-05-12

    申请号:US15989534

    申请日:2018-05-25

    发明人: Yan Fan Yan Sun Hong Xu

    摘要: The present invention discloses an L-type amylase variant and use thereof. The α-amylase variant is obtained by deleting the first N-terminal amino acid residue V from the α-amylase of B. licheniformis and replacing it with three other amino acid residues DGL. The α-amylase variant provided by the present invention has high catalytic activity under the acidic conditions of pH 5.0-5.8 and a high temperature of 100° C. or above. The acid resistance and thermal stability of these α-amylase variants are suitable for starch liquefaction.