Cloning and Sequencing of a Poly(
            <scp>dl</scp>
            -Lactic Acid) Depolymerase Gene from
            <i>Paenibacillus amylolyticus</i>
            Strain TB-13 and Its Functional Expression in
            <i>Escherichia coli</i>

Akutsu-Shigeno, Yukie; Teeraphatpornchai, Teerawat; Teamtisong, Kamonluck; Nomura, Nobuhiko; Uchiyama, Hiroo; Nakahara, Tadaatsu; Nakajima-Kambe, Toshiaki

doi:10.1128/aem.69.5.2498-2504.2003

Cited by 89 publications

(53 citation statements)

References 38 publications

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“…Recent studies including our work have demonstrated the presence of hydrolytic activity against polylactic acid (PLA), a biodegradable polyester, in several lipolytic enzymes and carboxylesterases315758. In this work, 26 purified metagenomic esterases were screened for PLA-degrading activity using an agarose plate assay with the emulsified PLA2 (M w 2 K).…”

Section: Resultsmentioning

confidence: 99%

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

Popović

Tran

Tchigvintsev

et al. 2017

Sci Rep

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Metagenomics has made accessible an enormous reserve of global biochemical diversity. To tap into this vast resource of novel enzymes, we have screened over one million clones from metagenome DNA libraries derived from sixteen different environments for carboxylesterase activity and identified 714 positive hits. We have validated the esterase activity of 80 selected genes, which belong to 17 different protein families including unknown and cyclase-like proteins. Three metagenomic enzymes exhibited lipase activity, and seven proteins showed polyester depolymerization activity against polylactic acid and polycaprolactone. Detailed biochemical characterization of four new enzymes revealed their substrate preference, whereas their catalytic residues were identified using site-directed mutagenesis. The crystal structure of the metal-ion dependent esterase MGS0169 from the amidohydrolase superfamily revealed a novel active site with a bound unknown ligand. Thus, activity-centered metagenomics has revealed diverse enzymes and novel families of microbial carboxylesterases, whose activity could not have been predicted using bioinformatics tools.

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Section: Resultsmentioning

confidence: 99%

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

Popović

Tran

Tchigvintsev

et al. 2017

Sci Rep

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“…and Tritirachium album has been reported (Jarerat & Tokiwa, 2001;Nakamura et al, 2001). Nevertheless, an esterase as well as a lipase have also been linked to PLA degradation (Hoshino & Isono, 2002;Akutsu-Shigeno et al, 2003). More recently, a PBS-degrading enzyme from Aspergillus oryzae and a cutinase-like enzyme from Cryptococcus sp.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of poly(l-lactic acid)-degrading enzymes fromAmycolatopsis orientalisssp.orientalis

Wang

Liu

et al. 2008

FEMS Microbiology Letters

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Polylactide or poly(l-lactic acid) (PLA) is a commercially promising material for use as a renewable and biodegradable plastic. Three novel PLA-degrading enzymes, named PLAase I, II and III, were purified to homogeneity from the culture supernatant of an effective PLA-degrading bacterium, Amycolatopsis orientalis ssp. orientalis. The molecular masses of these three PLAases as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were 24.0, 19.5 and 18.0 kDa, with the pH optima being 9.5, 10.5 and 9.5, respectively. The optimal temperature for the enzyme activities was 50-60 degrees C. All the purified enzymes could degrade high-molecular-weight PLA film as well as casein, and the PLA-degrading activities were strongly inhibited by serine protease inhibitors such as phenylmethylsulfonyl fluoride and aprotinin, but were not susceptive to chymostatin and pepstatin. Taken together, these data demonstrated that A. orientalis ssp. orientalis produces multiple serine-like proteases to utilize extracellular polylactide as a sole carbon source.

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“…strain 41 (Pranamuda et al, 2001), Amycolatopsis sp. strain K104-1 , and Kibdelosporangium aridum ; serine protease from Tritirachium album (Williams, 1981) and Actinomadura keratinilytica strain T16-1 (Sukkhum et al, 2009b); alkaline protease from Bacillus lentus, Bacillus subtilis and Bacillus licheniformis (Oda et al, 2000); lipase (esterase) from Bacillus smithii strain PL21 (Sakai et al, 2001); lipase from Paenibacillus amylolyticus strain TB-13 (Akutsu-Shigeno et al, 2003); lipase (cutinase) from Cryptococcus sp. strain S-2 (Masaki et al, 2005); and esterase from Geobacillus thermocatenulatus (thermophilic) (Tomita et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…strain 41 (Pranamuda et al, 2001), and Amycolatopsis orientalis ssp. orientalis (Li et al, 2008), which belong to the family Pseudonocardiaceae; Actinomadura keratinilytica strain T16-1 in the family Thermomonosporaceae (Sukkhum et al, 2009b); thermophilic Bacillus smithii in the family Bacillaceae (Sakai et al, 2001); and Paenibacillus amylolyticus strain TB-13 in the family Paenibacillaceae (Akutsu-Shigeno et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Characterization of poly(L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175

Hanphakphoom

Maneewong

Sukkhum

et al. 2014

J. Gen. Appl. Microbiol.

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on an emulsified PLLA agar plate at 50 C. Among the isolates, strain LP175 showed the highest PLLAdegrading ability. It was closely related to Laceyella sacchari, with 99.9% similarity based on the 16S rRNA gene sequence. The PLLA-degrading enzyme produced by the strain was purified to homogeneity by 48.1% yield and specific activity of 328 U·mg-protein-1 with a 15.3-fold purity increase. The purified enzyme was strongly active against specific substrates such as casein and gelatin and weakly active against Suc-(Ala) 3 -pNA. Optimum enzyme activity was exhibited at a temperature of 60 C with thermal stability up to 50 C and a pH of 9.0 with pH stability in a range of 8.5 10.5. Molecular weight of the enzyme was approximately 28.0 kDa, as determined by gel filtration and SDS-PAGE. The inhibitors phenylmethylsulfonyl fluoride (PMSF), ethylenediaminetetraacetate (EDTA), and ethylene glycolbis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid (EGTA) strongly inhibited enzyme activity, but the activity was not inhibited by 1 mM 1,10-phenanthroline (1,10-phen). The N-terminal amino acid sequences had 100% homology with thermostable serine protease (thermitase) from Thermoactinomyces vulgaris. The results obtained suggest that the PLLA-degrading enzyme produced by L. sacchari strain LP175 is serine protease.Key words: Laceyella sacchari; PLLA-degrading enzyme; Thermoactinomycetaceae; thermophilic filamentous bacteria IntroductionPoly(L-lactide) (PLLA); (C 3 H 4 O 2 )n is one of the aliphatic biodegradable polyesters derived from renewable resources such as corn, cassava, sugar cane, rice and potato through lactic acid fermentation, and it is also fully degradable by both microbial and enzymatic processes (Tokiwa et al., 2009;Gupta et al., 2007;Jarerat et al., 2006;Tokiwa and Calabia, 2006;Tomita et al., 2004). PLLA, as an environmentally friendly (eco-friendly or green ) product, has been developed on a large scale and is currently used for a wide range of applications, including packaging materials (Bhalla et al., 2007;Nolan-Itu Pty Ltd., 2002), medical applications (Jalil, 1990), agricultural products (Gross and Kalra, 2002;Sakai et al., 2001) and textiles.Most PLLA-degrading microorganisms are found in the bacterial order Actinomycetales, e.g. the families Pseudonocardiaceae (Pranamuda and Tokiwa, 1999;Pranamuda et al., 1997), Thermomonosporaceae (Sangwan and Wu, 2008;Sukkhum et al., 2009b), and Streptosporangiaceae (Sukkhum et al., 2009b). Apart from that, thermophilic bacteria in the families Thermoactinomycetaceae (Sukkhum et al., 2009b) and Firmicutes (Oda et al., 2000;Sakai et al., 2001), filamentous fungi in the genera Tritirachium and Paecilomyces (Sangwan and Wu, 2008), and yeast in the genus Cryptococcus have also been reported to be PLLA-degrading microorganisms.Many different types of enzymes are found in PLLAdegrading microorganisms, such as: protease from Amycola- Full PaperCharacterization of poly(L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175 (Received F...

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Cloning and Sequencing of a Poly( dl -Lactic Acid) Depolymerase Gene from Paenibacillus amylolyticus Strain TB-13 and Its Functional Expression in Escherichia coli

Cited by 89 publications

References 38 publications

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families

Purification and characterization of poly(l-lactic acid)-degrading enzymes fromAmycolatopsis orientalisssp.orientalis

Characterization of poly(L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175

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