Esterase mutants having polyester degradation activity and use thereof

{
  "publication_number": "US2026103692A1",
  "country": "US",
  "kind": "A1",
  "title": "Esterase mutants having polyester degradation activity and use thereof",
  "abstract": "Disclosed in the present disclosure are esterase mutants having polyester degradation activity and the use thereof. The esterase mutants are one of the following: an esterase A as shown in SEQ ID NO. 3, of which the glutamic acid at the 177th site is mutated into glutamine; or the asparagine at the 178th site is mutated into alanine; or the serine at the 180th site is mutated into threonine, leucine, and valine; or the isoleucine at the 181st site is mutated into valine, etc. Experiments show that a protein expressed by the gene of the esterase mutant of the present disclosure can be correctly folded and can be purified in a large quantity in an Escherichia coli system.",
  "claims": [
    "1. Esterase mutants having polyester degradation activity, wherein the esterase mutants are one of the following: MT-1: glutamic acid at the 177 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into glutamine; MT-2: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine; MT-3: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine; MT-4: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into leucine; MT-5: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine; MT-6: isoleucine at the 181 st site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine; MT-7: glycine at the 208 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine; MT-8: serine at the 209 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine; MT-9: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine; MT-10: glutamic acid at the 177 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into glutamine and serine at the 180 th site is mutated into leucine; MT-11: glutamic acid at the 177 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into glutamine and isoleucine at the 181 st site is mutated into valine; MT-12: glutamic acid at the 177 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into glutamine and glycine at the 208 th site is mutated into alanine; MT-13: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine and glutamic acid at the 177th site is mutated into glutamine; MT-14: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine and serine at the 180 th site is mutated into leucine; MT-15: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine and isoleucine at the 181 st site is mutated into valine; MT-16: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine and glycine at the 208 th site is mutated into alanine; MT-17: asparagine at the 178 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into alanine and serine at the 209 th site is mutated into threonine; MT-18: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and glutamic acid at the 177 th site is mutated into glutamine; MT-19: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and asparagine at the 178 th site is mutated into alanine; MT-20: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and isoleucine at the 181 st site is mutated into valine; MT-21: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and glycine at the 208 th site is mutated into alanine; MT-22: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and serine at the 209 th site is mutated into threonine; MT-23: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and serine at the 211 th site is mutated into tyrosine; MT-24: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into leucine and isoleucine at the 181 st site is mutated into valine; MT-25: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into leucine and glycine at the 208 th site is mutated into alanine; MT-26: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and glutamic acid at the 177 th site is mutated into glutamine; MT-27: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and asparagine at the 178 th site is mutated into alanine; MT-28: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and isoleucine at the 181 st site is mutated into valine; MT-29: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and glycine at the 208 th site is mutated into alanine; MT-30: serine at the 180 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and serine at the 209 th site is mutated into threonine; MT-31: isoleucine at the 181 st site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into valine and glycine at the 208 th site is mutated into alanine; MT-32: serine at the 209 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and glutamic acid at the 177 th site is mutated into glutamine; MT-33: serine at the 209 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and serine at the 180 th site is mutated into leucine; MT-34: serine at the 209 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and isoleucine at the 181 st site is mutated into valine; MT-35: serine at the 209 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into threonine and glycine at the 208 th site is mutated into alanine; MT-36: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and glutamic acid at the 177 th site is mutated into glutamine; MT-37: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and asparagine at the 178 th site is mutated into alanine; MT-38: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and serine at the 180 th site is mutated into leucine; MT-39: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and serine at the 180 th site is mutated into valine; MT-40: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and isoleucine at the 181 st site is mutated into valine; MT-41: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and glycine at the 208 th site is mutated into alanine; and MT-42: serine at the 211 th site of the amino acid sequence of an esterase A as shown in SEQ ID NO. 3 is mutated into tyrosine and serine at the 209 th site is mutated into threonine. 2. The esterase mutants having polyester degradation activity according to claim 1, wherein compared with the amino acid sequence of the esterase A as shown in SEQ ID NO. 3, involves the mutation sites involved in the amino acid sequence of the esterase mutant include at least three of the amino acid mutation sites. 3. Recombinant plasmids of encoding genes for the esterase mutants having polyester degradation activity according to claim 1. 4. Recombinant strains containing the recombinant plasmids according to claim 3. 5. Use of the esterase mutants having polyester degradation activity according to claim 1 in polyester hydrolysis. 6. A recombinant plasmids of encoding genes for the esterase mutants having polyester degradation activity, wherein compared with the amino acid sequence of the esterase A as shown in SEQ ID NO. 3, involves the mutation sites involved in the amino acid sequence of the esterase mutant include at least three of the amino acid mutation sites. 7. A use of the esterase mutants having polyester degradation activity, wherein compared with the amino acid sequence of the esterase A as shown in SEQ ID NO. 3, involves the mutation sites involved in the amino acid sequence of the esterase mutant include at least three of the amino acid mutation sites."
  ],
  "description_excerpt": "The present disclosure belongs to the field of genetic engineering of proteins, and particularly relates to esterase mutants having polyester degradation activity and use thereof.\n\nPolyester plastics play a significant role in modern society and are widely used in packaging, construction, textiles, transportation, electronic equipment, industrial machinery, etc., greatly changing human lifestyles. The polyester plastics have excellent properties such as light weight, good insulating properties, high strength and transparency, high thermal performance, and resistance to chemical corrosion. With the extensive use and consumption of polyester plastic products, more and more plastic waste products have been accumulated in environments, which have caused serious damage to global ecological environments and posed a serious threat to human health.\n\nBiological processes have emerged as a novel technology in recent years for the degradation and recycling of polyester plastics. It decomposes such organic matter under the action of biological entities (such as microorganisms, namely bacteria, fungi, and marine microalgae) or enzymes. Biological processes have the advantages of mild process conditions, relatively low energy input, and no need for hazardous chemical reagents and expensive machinery, making them a very promising option. Recently, scientists have reported a novel esterase that can hydrolyze polyesters. Compared with other polyester hydrolyzing enzymes, this esterase can exert its degradation function at a room temperature (equivalent to 30° C.). This esterase can degrade commercial high-crystallinity plastic bottles.",
  "cpc": [
    "C12N 9/18",
    "B09B 2101/75",
    "B09B 3/60",
    "C12N 15/70",
    "C12N 2800/22",
    "C12R 2001/19"
  ],
  "assignees": [
    "Tianjin University"
  ],
  "inventors": [
    "Zefang WANG",
    "Shen Wang",
    "Hanxiao ZHANG",
    "Yunjie XIAO",
    "Haitao Yang"
  ],
  "filing_date": "2023-05-29",
  "publication_date": "2026-04-16",
  "priority_date": "2023-02-27",
  "application_number": "US-202319491653-A",
  "cited_by_count": 0
}