Wilmar (shanghai) Biotechnology Research & Development Center Co., Ltd.

Yaoji Xuan

Qiwen Niu

Zhengjun Xu

Jun Xu

Wei Wu

Sha Liu

Sitian Gu

Yueyi Bao

Jinmin Li

Provided is a polypeptide having phospholipase C activity. The polypeptide has: 1) an amino acid sequence represented by SEQ ID No: 2, comprising amino acid substitutions occurred at one or more positions, wherein the one or more positions are selected from positions 6, 8, 10, 104, and 205 in the amino acid sequence represented by SEQ ID No: 2 or any combination thereof; or 2) having at least 80% sequence identity with 1), and at least one of positions 6, 8, 10, 104 and 205 being different from positions 6, 8, 10, 104, and 205 in the amino acid sequence represented by SEQ ID No: 2. Provided are a nucleic acid molecule for encoding the polypeptide, a vector comprising the nucleic acid molecule, and a cell comprising the nucleic acid molecule or the vector. Provided are uses of the polypeptide, the nucleic acid molecule, the vector, and the cell.

Polypeptide having phospholipase C activity and use thereof

Provided in the present invention is a phospholipase C mutant with high enzyme activity, a polypeptide with the sequence as shown in SEQ ID NO:7, or a polypeptide derived from the phospholipase C formed by performing substitution, deletion or addition of one or a plurality of amino acids on the polypeptide of SEQ ID NO:7 while retaining the phospholipase C activity provided by SEQ ID NO:7. The phospholipase C mutant of the present invention can improve degumming efficiency and increase the yield of diacylglycerol (DAG) during degumming.

Phospholipase C mutant with high enzyme activity

Provided is a mutant of the wild type phosphatidylcholine-specific phospholipase C of. The mutations involved comprise the amino acid residue at position 63 being mutated from asparagine to aspartic acid, the amino acid residue at position 131 being mutated from asparagine to serine, and the amino acid residue at position 134 being mutated from asparagine to aspartic acid, and may comprise the amino acid residue at position 56 being mutated from tyrosine to alanine, lysine, asparagine, glutamine, histidine or tryptophan, and further, may also comprise the amino acid residue at position 106 being mutated from methionine to valine. Also provided are a polynucleotide molecule encoding the mutant, a nucleic acid construct and a host cell comprising the polynucleotide molecule, a composition comprising the mutant, and the use of the mutant, the polynucleotide molecule, the nucleic acid construct and the host cell.

Efficient phospholipase C mutant that does not rely on zinc ions

The present application provides mutants of wild type phospholipase C (PLC) specific to phosphatidylcholine from. The related mutations include mutation of asparagine at position 63 to another amino acid, also including mutation of arginine at position 20 to histidine and of alanine at position 83 to aspartic acid. The present application also provides a nucleic acid molecule encoding the mutant, a vector containing the nucleic acid molecule, and a cell containing the nucleic acid molecule or vector. The present application also provides uses of the mutant, nucleic acid molecule vector, and cell.

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Shanghai, China

Yaoji Xuan