Evidence map›Paper›PMID 37507390›Full record

ArticleNature communications2023

Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties.

Hwaseok Hong, Dongwoo Ki, Hogyun Seo, Jiyoung Park, Jaewon Jang, Kyung-Jin Kim

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
7.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 106 citations in OpenAlex.

  1. Pooled it
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  15. Improved Enzymatic Properties of Chitosanase CsnMY002 fromInternational journal of molecular sciences · 2025
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  18. In Silico Analysis and Biochemical Characterization ofJournal of microbiology and biotechnology · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Hwaseok Hong *School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu, 41566, Republic of Korea.ORCID 0000-0002-6010-9695
Dongwoo Ki *School of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu, 41566, Republic of Korea.ORCID 0000-0002-5454-8616
Hogyun SeoSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu, 41566, Republic of Korea.ORCID 0000-0002-8465-8373
Jiyoung ParkSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu, 41566, Republic of Korea.ORCID 0000-0002-8126-1012
Jaewon JangInstitute of Biotechnology, CJ CheilJedang Co., Suwon-si, Gyeonggi-do, 16495, Republic of Korea.ORCID 0009-0006-7904-6897
Kyung-Jin KimSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, KNU Institute for Microorganisms, Kyungpook National University, Daegu, 41566, Republic of Korea. kkim@knu.ac.kr.ORCID 0000-0002-0375-2561
Kyungpook National University · KRCJ CheilJedang (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Excessive polyethylene terephthalate (PET) waste causes a variety of problems. Extensive research focused on the development of superior PET hydrolases for PET biorecycling has been conducted. However, template enzymes employed in enzyme engineering mainly focused on IsPETase and leaf-branch compost cutinase, which exhibit mesophilic and thermophilic hydrolytic properties, respectively. Herein, we report a PET hydrolase from Cryptosporangium aurantiacum (CaPETase) that exhibits high thermostability and remarkable PET degradation activity at ambient temperatures. We uncover the crystal structure of CaPETase, which displays a distinct backbone conformation at the active site and residues forming the substrate binding cleft, compared with other PET hydrolases. We further develop a CaPETase

Indexed as

ActinomycetalesHydrolasesEnzyme StabilityHydrolysisPolyethylene TerephthalatesHydrolasesPolyethylene Terephthalates

Identifiers

PMID37507390
PMCPMC10382486
OpenAlexW4385342215

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.