Enhancing secretion of polyethylene terephthalate hydrolase PETase in
            <i>Bacillus subtilis</i>
            WB600 mediated by the SP
            <sub>amy</sub>
            signal peptide

Wang, Nan; Guan, Feifei; Lv, Xiang; Han, Dongfei; Zhang, Yuhong; Wu, Ningfeng; Xia, Xiaole; Tian, Jian

doi:10.1111/lam.13312

Cited by 37 publications

(19 citation statements)

References 23 publications

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“…This prospect prompted many researchers to optimize the process of PET degradation via PETase. This included increasing the enzymes’ activity via mutagenesis, [19–23] improving the secretion of PETase, [24–26] exploring different expression systems, [27] and adding synthetic surfactants to the reaction [28] …”

Section: Introductionmentioning

confidence: 99%

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

et al. 2021

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The enzymatic degradation of polyethylene terephthalate (PET) is a promising new approach for the environmentally friendly recycling of PET waste, but so far, low degradation rates paired with releatively high costs have limited the economic feasibility of this method. Here we present the construction of a new bacterial whole‐cell biocatalyst utilizing a new inverse autotranspoter based surface display of PETase in E. coli. The resulting catalyst allows an extremely easy production of large amounts of enzyme and a five times more effective degradation of PET at a lower temperature of 25 °C compared to free PETase at 30 °C. Additionally, we demonstrate how rhamnolipids, which are environmentally benign and can be cost‐effectively produced using strains of E. coli, can be used to amplify the hydrolysis rates of PET even further, presumably by acting as mediators between PETase and PET. Cells displaying PETase in combination with externally supplied rhamnolipids outperformed free PETase by a factor of 16, allowing the degradation of highly crystalline post‐consumer PET waste to an extent of 8 % within 3 days at room temperature.

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Section: Introductionmentioning

confidence: 99%

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

et al. 2021

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“…Enzymatic degradation is currently considered an ideal method for PET degradation, and shows promise for large-scale PET waste degradation. Previous studies engineered and compared different signal peptides to enhance extracellular production of PETase in E. coli ( Cui et al, 2021 ; Shi et al, 2021 ) and B. subtilis ( Huang et al, 2018 ; Wang et al, 2020 ). These studies emphasized the importance of signal peptides in the secretion of heterologous protein.…”

Section: Discussionmentioning

confidence: 99%

“…At present, several chassis cells, including Escherichia coli ( Seo et al, 2019 ; Shi et al, 2021 ), Bacillus sp. ( Huang et al, 2018 ; Wang et al, 2020 ), Pichia pastoris ( Chen et al, 2020 ), and marine microalgae ( Moog et al, 2019 ; Kim et al, 2020 ) have been reported to be capable of expressing and secreting PETase. These results established a theoretical basis for the design of PET biodegradation systems.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of PET Degradation Using Artificial Microbial Consortia

Chang

et al. 2021

Front. Microbiol.

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Polyethylene terephthalate (PET) biodegradation is regarded as an environmentally friendly degradation method. In this study, an artificial microbial consortium composed of Rhodococcus jostii, Pseudomonas putida and two metabolically engineered Bacillus subtilis was constructed to degrade PET. First, a two-species microbial consortium was constructed with two engineered B. subtilis that could secrete PET hydrolase (PETase) and monohydroxyethyl terephthalate hydrolase (MHETase), respectively; it could degrade 13.6% (weight loss) of the PET film within 7 days. A three-species microbial consortium was further obtained by adding R. jostii to reduce the inhibition caused by terephthalic acid (TPA), a breakdown product of PET. The weight of PET film was reduced by 31.2% within 3 days, achieving about 17.6% improvement compared with the two-species microbial consortium. Finally, P. putida was introduced to reduce the inhibition caused by ethylene glycol (EG), another breakdown product of PET, obtaining a four-species microbial consortium. With the four-species consortium, the weight loss of PET film reached 23.2% under ambient temperature. This study constructed and evaluated the artificial microbial consortia in PET degradation, which demonstrated the great potential of artificial microbial consortia in the utilization of complex substrates, providing new insights for biodegradation of complex polymers.

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“…For example, combining SP amy signal peptides and promoter P43 in Bacillus subtilis yielded an IsPETase with greater PET degradation activity than that expressed from E. coli, due to the maximized extracellular expression of IsPETase. [44] Pretreating PET materials with ionic surfactant has been found to be an important strategy for enhancing enzymatic hydrolysis efficiency. For instance, pre-incubation of a lowcrystallinity PET film with an anion surfactant for 1 hour before adding IsPETase could increase the degradation effect 120fold.…”

Section: Novelty Optimization Methods For Ispetasementioning

confidence: 99%

“…Expressing Is PETase in different hosts with optimal signal peptides and promoters can lead to different degradation efficiency. For example, combining SP amy signal peptides and promoter P43 in Bacillus subtilis yielded an Is PETase with greater PET degradation activity than that expressed from E. coli , due to the maximized extracellular expression of Is PETase [44] …”

Section: Engineering Efforts On Ispetasementioning

confidence: 99%

IsPETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

Kan

Luo

et al. 2021

ChemBioChem

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Poly(ethylene terephthalate) (PET) is one of the most widely used synthetic polyesters, but also a major cause of plastic pollution. Because the chemical degradation of PET would be uneconomical and rather burdensome, considerable efforts have been devoted to exploring enzymatic processes for the disposal of PET waste. Many PET-hydrolyzing enzymes have been reported in recent decades, some of which demonstrate excellent potential for industrial applications. This review sets out to summarize the state of investigation into IsPETase, a cutinase-like enzyme from Ideonella sakaiensis possessing ability to degrade crystalline PET, and to gain further insight into the structure-function relationship of IsPETase. Benefiting from the continuing identification of novel cutinase-like proteins and growing availability of the engineered IsPETase, we may anticipate future developments in this type of enzyme would generate suitable biocatalyst for industrial use.

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Enhancing secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis WB600 mediated by the SP _amy signal peptide

Cited by 37 publications

References 23 publications

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

Evaluation of PET Degradation Using Artificial Microbial Consortia

IsPETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

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Enhancing secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis WB600 mediated by the SP amy signal peptide

Cited by 37 publications

References 23 publications

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

Highly Crystalline Post‐Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole‐Cell Biocatalyst

Evaluation of PET Degradation Using Artificial Microbial Consortia

IsPETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

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Enhancing secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis WB600 mediated by the SP _amy signal peptide