Abstract: A group of viral vectors including: first viral vector, wherein first viral vector carries first nucleic acid molecule, and the first nucleic acid molecule encodes envelope protein; second viral vector, wherein second viral vector carries second nucleic acid molecule, the second nucleic acid molecule encodes fusion protein, the fusion protein includes single-chain antibody and C-terminal domain of envelope protein, the C-terminal domain of envelope protein includes transmembrane region and intracellular region of envelope protein, the C-terminus of single-chain antibody connects with N-terminus of C-terminal domain of envelope protein, the single-chain antibody targets a specific antigen; first nucleic acid molecule and second nucleic acid molecule are arranged to express envelope protein and fusion protein, and the envelope protein and the fusion protein are in non-fusion form.

Abstract: A PET hydrolase having improved thermal stability is disclosed. The PET hydrolase has a modified amino acid sequence of SEQ ID NO: 2 or a modified amino acid sequence with at least 80% sequence identity of SEQ ID NO: 2, wherein the modification is a substitution of asparagine at position 248 or a corresponding position with proline.

Abstract: A PET hydrolase having improved thermal stability is disclosed. The PET hydrolase has a modified amino acid sequence of SEQ ID NO: 2 or a modified amino acid sequence with at least 80% sequence identity of SEQ ID NO: 2, wherein the modification is a substitution of asparagine at position 248 or a corresponding position with proline.

Abstract: Disclosed is a process for the preparation of bistriphenylsilyl chromate, wherein triphenylchlorosilane, potassium dichromate and any one selected from alkali metal oxides, alkali hydroxides and alkali metal carbonates are reacted in, as solvent, a mixture of glacial acetic acid and a hydrocarbon solvent at a certain temperature, whereby bistriphenylsilyl chromate having high purity can be obtained with high yield.