The application relates to a
glutamine transaminase with improved
thermal stability and application thereof, and belongs to the technical field of
genetic engineering and
protein engineering. The variant comprises a leading
peptide and a mature polypeptide. The parent mature polypeptide of the variant corresponds to the region of the N terminal 4th to 13th of the wild-type SmTG mature polypeptide, and is replaced by a target sequence composed of n repeating units connected head to
tail. The repeating unit has at least 80% identity with the original sequence, and is independently substituted by a specific
amino acid at the corresponding 10th position, wherein at least two repeating units have different types of substitution amino acids at the 10th position. The remaining
amino acid region of the parent mature polypeptide has at least 85%
sequence identity with the remaining region of the wild-type SmTG mature polypeptide. Compared with the parent, the variant has a
glutamine transaminase activity, and the thermal inactivation half-life at 60 DEG C is significantly prolonged by at least 0.3 times.