Polyester hydrolysis is enhanced by a truncated esterase: Less is more

Biundo, Antonino; Ribitsch, Doris; Steinkellner, Georg; Gruber, Karl; Guebitz, Georg M.

doi:10.1002/biot.201600450

Cited by 32 publications

(20 citation statements)

References 26 publications

(33 reference statements)

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“…Degradation of polyester. Amorphous PET films (0.5 × 1 cm) were thoroughly washed 27 . Washed PET films were incubated with 5 µM EstA in 0.1 M potassium phosphate buffer pH 7 at 50°C and 100 rpm for 120 h. Supernatants were collected and analysed by high performance liquid chromatography (HPLC) (Agilent Technologies, USA) 27 .…”

Section: Methodsmentioning

confidence: 99%

Polyphenol oxidases exhibit promiscuous proteolytic activity

et al. 2020

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Tyrosinases catalyse both the cresolase and catecholase reactions for the formation of reactive compounds which are very important for industrial applications. In this study, we describe a proteolytic activity of tyrosinases. Two different tyrosinases originating from mushroom and apple are able to cleave the carboxylesterase EstA. The cleavage reaction correlates with the integrity of the active site of tyrosinase and is independent of other possible influencing factors, which could be present in the reaction. Therefore, the cleavage of EstA represents a novel functionality of tyrosinases. EstA was previously reported to degrade synthetic polyesters, albeit slowly. However, the EstA truncated by tyrosinase shows higher degradation activity on the non-biodegradable polyester polyethylene terephthalate (PET), which is a well-established environmental threat.

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Section: Methodsmentioning

confidence: 99%

Polyphenol oxidases exhibit promiscuous proteolytic activity

et al. 2020

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“…The fusion of polymer and cellulose binding domains (Ribitsch et al ., ) or hydrophobins (Ribitsch et al ., ) also enhanced the adsorption of cutinases to the surface of PET and resulted in higher yields of hydrolysis products. A truncation of 71 N‐terminal residues of an esterase from Clostridium botulinum exposed a hydrophobic patch, which facilitated its adsorption to PET and improved its hydrolytic activity (Biundo et al ., ).…”

Section: Enzymatic Degradation Of Petmentioning

confidence: 97%

Microbial enzymes for the recycling of recalcitrant petroleum‐based plastics: how far are we?

Wei

Zimmermann

2017

Microbial Biotechnology

604

362

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SummaryPetroleum‐based plastics have replaced many natural materials in their former applications. With their excellent properties, they have found widespread uses in almost every area of human life. However, the high recalcitrance of many synthetic plastics results in their long persistence in the environment, and the growing amount of plastic waste ending up in landfills and in the oceans has become a global concern. In recent years, a number of microbial enzymes capable of modifying or degrading recalcitrant synthetic polymers have been identified. They are emerging as candidates for the development of biocatalytic plastic recycling processes, by which valuable raw materials can be recovered in an environmentally sustainable way. This review is focused on microbial biocatalysts involved in the degradation of the synthetic plastics polyethylene, polystyrene, polyurethane and polyethylene terephthalate (PET). Recent progress in the application of polyester hydrolases for the recovery of PET building blocks and challenges for the application of these enzymes in alternative plastic waste recycling processes will be discussed.

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“…As an example, replacement of serine and tyrosine with the more hydrophobic cysteine and phenylalanine in PHB depolymerase from R. pickettii T1, promoted adsorption of the enzyme onto the PHB surface and stimulated the efficiency of plastic hydrolysis [73,74]. In another study, after removing the N-terminal domain in a Clostridium botulinum esterase, a covered hydrophobic surface area became accessible for PET sorption, resulting in higher enzymatic hydrolysis [75]. However, introducing too many hydrophobic residues might impair catalytic activity due to enzyme aggregation or protein structure disruption caused by concomitant additional intermolecular hydrophobic interactions [72].…”

Section: Trends Trends In In Biotechnology Biotechnologymentioning

confidence: 99%

Enzyme discovery and engineering for sustainable plastic recycling

Zhu

Wang

Wei

2022

Trends in Biotechnology

203

114

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The drastically increasing amount of plastic waste is causing an environmental crisis that requires innovative technologies for recycling post-consumer plastics to achieve waste valorization while meeting environmental quality goals. Biocatalytic depolymerization mediated by enzymes has emerged as an efficient and sustainable alternative for plastic treatment and recycling. A variety of plasticdegrading enzymes have been discovered from microbial sources. Meanwhile, protein engineering has been exploited to modify and optimize plastic-degrading enzymes. This review highlights the recent trends and up-to-date advances in mining novel plastic-degrading enzymes through state-of-the-art omics-based techniques and improving the enzyme catalytic efficiency and stability via various protein engineering strategies. Future research prospects and challenges are also discussed. Biocatalysis as an Emerging Solution for the Global Plastic Waste ChallengePlastic materials play a revolutionary role in the modern world, although the enormous manufacture and extensive use of plastic commodities inevitably generate an extraordinary amount of post-consumer plastic waste. Around 12 000 million metric tons of plastic waste are predicted to accumulate in landfills and the natural environment by 2050 [1]. Improper handling of plastic waste has caused a grand environmental challenge. The debris of plastic waste, especially microplastics (see Glossary), can impose hazardous effects on various organisms and eventually threaten human well-being [2-5]. In addition, the degradation resistance of plastics further escalates their adverse environmental impacts [6]. Therefore, it is urgent to develop innovative technologies for treatment and recycling of post-consumer plastics, to achieve both waste valorization and environmental protection.Enzymatic biocatalysis has gained increasing attention as an eco-friendly alternative to conventional plastic treatment and recycling methods (Box 1) [7]. To date, various microbial plastic-degrading enzymes have been discovered, representing promising biocatalyst candidates for plastic depolymerization. Considering the ubiquity of plastics in different ecosystems and the tremendous metabolic and genetic diversity of microorganisms, microbial communities in various habitats have likely evolved capabilities in plastic decomposition and utilization. The plastic-degrading enzymes identified so far might only account for a small portion of the enzymes relevant to plastic depolymerization in the environment. Therefore, it is of ever-growing interest to explore diverse environments to discover new plastic-degrading enzymes with desirable properties and functionalities. However, naturally occurring plasticdegrading enzymes are not well suited for synthetic plastic degradation in industrial applications due to poor thermostability and low catalytic activity. Particularly, synthetic plastic materials usually possess distinct physical and chemical properties (e.g., high crystallinity) that render them more resistant to...

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Polyester hydrolysis is enhanced by a truncated esterase: Less is more

Cited by 32 publications

References 26 publications

Polyphenol oxidases exhibit promiscuous proteolytic activity

Polyphenol oxidases exhibit promiscuous proteolytic activity

Microbial enzymes for the recycling of recalcitrant petroleum‐based plastics: how far are we?

Enzyme discovery and engineering for sustainable plastic recycling

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