Evidence map›Paper›PMID 42850475›Full record

ArticleApplied microbiology and biotechnology2026

A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation.

Hadjira Bounabi, Bilal Yahiaoui, Meriem Gasmi, Meroua Safa Mechouche, Nico Bäse, Marno Gurschke, Rebecka Molitor, Pablo Pérez-García, Wolfgang R Streit

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Article in Applied microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Hadjira BounabiDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany.
Bilal YahiaouiLaboratory of Applied Microbiology, Department of Microbiology, Faculty of Natural and Life Sciences, Ferhat Abbas University, 19000, Setif, Algeria.
Meriem GasmiBiotechnology Laboratory, Higher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, 25100, Constantine, Algeria.
Meroua Safa MechoucheBiotechnology Laboratory, Higher National School of Biotechnology Taoufik Khaznadar, Nouveau Pôle Universitaire Ali Mendjeli, 25100, Constantine, Algeria.
Nico BäseDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany.
Marno GurschkeDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany.
Rebecka MolitorInstitute of Molecular Enzyme Technology, Heinrich-Heine-University Düsseldorf, Forschungszentrum Jülich, Jülich, Germany.
Pablo Pérez-GarcíaDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany.
Wolfgang R StreitDepartment of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609, Hamburg, Germany. wolfgang.streit@uni-hamburg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biodegradation of polyethylene terephthalate (PET), and its derived intermediate breakdown products, represents a core focus of multidisciplinary research. While Ideonella sakaiensis PETase (IsPETase) and leaf-compost cutinase (LCC) efficiently depolymerize PET, many other PET-active hydrolases display stronger activity toward soluble PET intermediates such as bis- and mono(2-hydroxyethyl) terephthalate (BHET and MHET). Here, we describe a versatile carboxylesterase derived from Bacillus halotolerans (BhEstB). BhEstB is structurally related to BsEstB from B. subtilis but divergent from canonical PETases and most characterized MHETases, including IsMHETase, while clustering more closely with carboxylesterases such as TfCa. BhEstB displayed broad esterase activity toward pNP-esters, with maximum activity at pH 8 and 20-30 °C. Although it showed modest overall activity on the bulk polymer, BhEstB significantly outperformed the engineered variant LCC

Indexed as

BacillusCarboxylesteraseEsterasesPolyethylene TerephthalatesBacterial ProteinsBiodegradation, EnvironmentalBurkholderialesCarboxylic Ester HydrolasesEnzyme StabilityHydrogen-Ion ConcentrationKineticsSubstrate SpecificityTemperatureBacterial ProteinsCarboxylesteraseCarboxylic Ester HydrolasesEsterasesPolyethylene TerephthalatesBHETaseEnzyme kineticsMHETasePETasePlastic biodegradationTerephtalate

Identifiers

PMID42850475

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Registered trials

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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.