Characterization and its Potential Application of Two Esterases Derived from the Arctic Sediment Metagenome

Jeon, Jeong Ho; Kim, Jun-Tae; Kang, Sung Gyun; Lee, Jung-Hyun; Kim, Sang-Jin

doi:10.1007/s10126-008-9145-2

Cited by 88 publications

(49 citation statements)

References 48 publications

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“…Six of them (Lip5.1_5, Lip5.3_3, Lip5.5_4, Lip5.13_3, Lip5.14_3, and Lip5.19_3) have been assigned to family IV. This esterase family appears to be highly represented in marine metagenomes, as out of 34 esterases identified in 8 screens of marine metagenomes, 27 have been classified as family IV esterases (39,(45)(46)(47)(48)(49)(50)(51). We have assigned one of the esterase loci identified here (Lip5.13_1) to esterase family V, which appears to count relatively few members.…”

Section: Discussionmentioning

confidence: 74%

Identification and Characterization of a Halotolerant, Cold-Active Marine Endo-β-1,4-Glucanase by Using Functional Metagenomics of Seaweed-Associated Microbiota

Martin

Biver

Steels

et al. 2014

Appl Environ Microbiol

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A metagenomic library was constructed from microorganisms associated with the brown alga Ascophyllum nodosum. Functional screening of this library revealed 13 novel putative esterase loci and two glycoside hydrolase loci. Sequence and gene cluster analysis showed the wide diversity of the identified enzymes and gave an idea of the microbial populations present during the sample collection period. Lastly, an endo-␤-1,4-glucanase having less than 50% identity to sequences of known cellulases was purified and partially characterized, showing activity at low temperature and after prolonged incubation in concentrated salt solutions. Previous surveys have revealed that less than 1% of existing microorganisms can be studied by traditional culturing methods. This leaves most microorganisms and their by-products unknown and unexploited (1, 2) and explains why metagenomics, a culture-independent approach using total microbial genomes from environmental samples, has met with great success over the past decade (3, 4). Sequence-based metagenomics has already provided information about the composition, organization, function, and hierarchy of microbial communities in particular habitats (5). On the other hand, functional genomics applied to metagenomic libraries from diverse environments has led to the discovery of many new enzymes and bioactive compounds and to substantial enrichment of genome databases. To date, most of the enzymes brought to light through metagenomics have been derived from soil (6-9) and gut (10-13) samples.Marine microorganisms represent promising candidate sources of original biocatalysts, as they are exposed to extreme conditions of temperature, pressure, salinity, nutrient availability, etc. Hence, functional screening of marine microbial populations should yield new enzymes with specific and unique physiological and biochemical properties, produced by organisms far different from those usually described in terrestrial environments (14). New enzymes have already been identified in marine metagenomic libraries from seawater samples (15, 16) and from microorganisms in symbiosis with marine organisms such as sponges and corals (17). To our knowledge, however, nobody has yet performed functional screening of metagenomic libraries from algal microbial communities. As algal microbial biofilms are in constant interaction with algal biomass, they represent an interesting source of enzymes and other active compounds (18). Sequence-based studies have already revealed the importance and functions of microbial communities living on the surfaces of algae, showing tight interdependence between algae and their biofilms (19-21). Furthermore, many genes coding for enzymes involved in hydrolyzing algal biomass, such as cellulases, xylanases, ␣-amylases, and specific algal polysaccharidases (e.g., agarases, carrageenases, and alginate lyases), have been identified from cultivable marine bacteria (22,23). Only a few such enzymes have been found in marine metagenomes by functional screening. For example, no cellulase gene...

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Section: Discussionmentioning

confidence: 74%

Identification and Characterization of a Halotolerant, Cold-Active Marine Endo-β-1,4-Glucanase by Using Functional Metagenomics of Seaweed-Associated Microbiota

Martin

Biver

Steels

et al. 2014

Appl Environ Microbiol

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“…Furthermore, BpNDT is an interesting biocatalyst from an industrial point of view, since it can perform at 40 • C but also at low temperatures, minimizing undesirable chemical reactions that can occur at higher temperatures and protecting heat-labile substrates [61].…”

Section: Resultsmentioning

confidence: 99%

2′-Deoxyribosyltransferase from Bacillus psychrosaccharolyticus: A Mesophilic-Like Biocatalyst for the Synthesis of Modified Nucleosides from a Psychrotolerant Bacterium

et al. 2018

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Structure-function relationships of a novel 2 -deoxyribosyltransferase from the psychrotolerant bacterium Bacillus psychrosaccharolyticus (BpNDT) have been exhaustively studied by biochemical and high resolution crystallographic analyses. Despite BpNDT exhibiting some structural features characteristic of cold-adapted enzymes such as localized flexibility in critical loops, its biochemical properties are typical of mesophilic enzymes. BpNDT is a highly symmetrical homohexamer with tightly associated subunits that possesses flexible and short loops bordering the active sites. The catalytic center is essentially identical to that of other mesophilic homologues. Moreover, BpNDT shows that it is a mesophilic-like enzyme since it is not heat-labile and exhibits an apparent unfolding temperature (T m ) of 49 • C, being active during 96 h at 40 and 50 • C. Finally, BpNDT synthesizes natural and modified nucleosides, with preference for purines as acceptors and pyrimidine nucleosides as donors. Remarkably, the synthesis of several therapeutic nucleosides has been efficiently carried out. In this sense, 5-hydroxymethyl-2 -deoxyuridine (5-HMdUrd), 7-deaza-6-hydroxypurine-2 -deoxyriboside (7-DHPdRib) and theophylline-2 -deoxyriboside were synthesized for the first time by an NDT enzyme, showing the biotechnological interest of BpNDT.

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“…EstIM1 was strongly inhibited by Hg 2+ , Zn 2+ , SDS, and Triton X-100, whereas little or no inactivation was observed upon incubation with the other ions and detergents tested ( Table 2). The eVects of Fe 2+ and Mn 2+ on EstIM1 activity diVer from those on the EstAT1 and EstAT11 esterases obtained from the Arctic sediment metagenome [24,25]. EstIM1 was stable in methanol (15 and 30%, both v/v), ethanol (15% v/v), and DMSO (30% v/v), retaining over 80% of activity (Table 3).…”

Section: Discussionmentioning

confidence: 96%

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

Rim

Han

et al. 2012

Journal of Industrial Microbiology and Biotechnology

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A novel lipolytic enzyme was isolated from a metagenomic library after demonstration of lipolytic activity on an LB agar plate containing 1% (w/v) tributyrin. A novel esterase gene (estIM1), encoding a lipolytic enzyme (EstIM1), was cloned using a shotgun method from a pFosEstIM1 clone of the metagenomic library, and the enzyme was characterized. The estIM1 gene had an open reading frame (ORF) of 936 base pairs and encoded a protein of 311 amino acids with a molecular mass 34 kDa and a pI value of 4.32. The deduced amino acid sequence was 62% identical to that of an esterase from an uncultured bacterium (ABQ11271). The amino acid sequence indicated that EstIM1 was a member of the family IV of lipolytic enzymes, all of which contain a GDSAG motif shared with similar enzymes of lactic acid microorganisms. EstIM1 was active over a temperature range of 1-50°C, at alkaline pH. The activation energy for hydrolysis of p-nitrophenyl propionate was 1.04 kcal/mol, within a temperature range of 1-40°C. The activity of EstIM1 was about 60% of maximal even at 1°C, suggesting that EstIM1 is efficiently cold-adapted. Further characterization of this cold-adapted enzyme indicated that the esterase may be very valuable in industrial applications.

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Characterization and its Potential Application of Two Esterases Derived from the Arctic Sediment Metagenome

Cited by 88 publications

References 48 publications

Identification and Characterization of a Halotolerant, Cold-Active Marine Endo-β-1,4-Glucanase by Using Functional Metagenomics of Seaweed-Associated Microbiota

Identification and Characterization of a Halotolerant, Cold-Active Marine Endo-β-1,4-Glucanase by Using Functional Metagenomics of Seaweed-Associated Microbiota

2′-Deoxyribosyltransferase from Bacillus psychrosaccharolyticus: A Mesophilic-Like Biocatalyst for the Synthesis of Modified Nucleosides from a Psychrotolerant Bacterium

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

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