Characterization and gene cloning of a cold-active cellulase from a deep-sea psychrotrophic bacterium Pseudoalteromonas sp. DY3

Zeng, Runying; Xiong, Peng-Jun; Wen, Jin

doi:10.1007/s00792-005-0475-y

Cited by 65 publications

(39 citation statements)

References 15 publications

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“…This provides only a small glimpse into the exceptional adaptation of the microbiota to the Antarctic environment. The Pseudoalteromonas isolates in particular showed great potential for bioprospecting of all screened enzymatic activities, a result that agrees with those from previous studies (Holmströ m & Kjelleberg 1999;Hoyoux et al 2001;Truong et al 2001;Tutino et al 2002;Zeng et al 2006). Beyond the biotechnological potential, the high proportion of isolates belonging to the genus Pseudoalteromonas and the versatile hydrolytic activities detected in this group also suggest that these organisms may play an important role in polymer hydrolysis in cold environments.…”

Section: Discussionsupporting

confidence: 89%

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Tropeano¹,

Coria²,

Turjanski³

et al. 2012

Polar Research

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Affiliations of the dominant culturable bacteria isolated from Potter Cove, South Shetland Islands, Antarctica, were investigated together with their production of cold-active hydrolytic enzymes. A total of 189 aerobic heterotrophic bacterial isolates were obtained at 4°C and sorted into 63 phylotypes based on their amplified ribosomal DNA restriction analysis profiles. The sequencing of the 16S rRNA genes of representatives from each phylotype showed that the isolates belong to the phyla Proteobacteria (classes Alpha- and Gamma-proteobacteria), Bacteroidetes (class Flavobacteria), Actinobacteria (class Actinobacteria) and Firmicutes (class Bacilli). The predominant culturable group in the site studied belongs to the class Gammaproteobacteria, with 65 isolates affiliated to the genus Pseudoalteromonas and 58 to Psychrobacter. Among the 189 isolates screened, producers of amylases (9.5%), pectinases (22.8%), cellulases (14.8%), CM-cellulases (25.4%), xylanases (20.1%) and proteases (44.4%) were detected. More than 25% of the isolates produced at least one extracellular enzyme, with some of them producing up to six of the tested extracellular enzymatic activities. These results suggest that a high culturable bacterial diversity is present in Potter Cove and that this place represents a promising source of biomolecules

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Section: Discussionsupporting

confidence: 89%

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Tropeano¹,

Coria²,

Turjanski³

et al. 2012

Polar Research

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“…The optimum temperature of EG-PY2 was lower than that of CelX isolated from a deep sea-bacterium Pseudoalteromonas sp. and of EglC isolated from a symbiotic bacterium Citrobacter farmeri (Zeng et al 2006;Bai et al 2016). The cold activity pattern of EG-PY2 did not change markedly between 20 and 50 o C, which is similar to those reported for reasons of the endoglucanases Cel9P, EG5C and PgluE8 from Paenibacillus sp.…”

Section: Properties Of Eg-py2supporting

confidence: 84%

“…Furthermore, only a few bacterial cold-active cellulases have been described, such as, Pseudoalteromonas sp., Pseudomonas sp., or Paenibacillus sp. from marine environments or feces (Zeng et al 2006;Fu et al 2010;Yang and Dang 2011;Dong et al 2016), and Paenibacillus sp. from a cold lake sediment (Dhar et al 2015).…”

Section: Introductionmentioning

confidence: 99%

A cold-active acidophilic endoglucanase of Paenibacillus sp. Y2 isolated from soil in an alpine region

Lee

Seo

et al. 2017

JABC

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A cellulolytic strain Y2 was isolated from soil obtained in the Canadian Alpine region. The isolate was identified as Paenibacillus sp. Y2 by 16S rRNA sequencing. When grown in LB medium supplemented with carboxymethyl-cellulose (CMC), CMCase production increased to 122.0% of that observed in LB without CMC. Culture supernatant was concentrated by ultrafiltration and 80% ammonium sulfate precipitates were separated by HiTrap Q and CHT-II chromatography. The purified enzyme (EG-PY2) showed a homogeneous single band and the molecular mass was estimated to be 38 kDa by SDS-PAGE. Optimum pH and temperature of the enzyme were 4.5 and 30 o C, respectively. The half-life of enzyme activity at 50 was 140.7 min, but the enzyme was drastically inactivated within 5 min at 55 , and EDTA. The enzyme was activated to 211.5% in the presence of 0.5 M of NaCl and greatly tolerant to 3.15 M of NaCl. The enzyme showed 2.98 times higher β-glucanase activity than CMCase activity. Based on these results, it can be concluded that EG-PY2 is an acidophilic, cold-active, and halotolerant endoglucanase. The authors suggest it is considered to be useful for various industrial applications, such as, fruit juice clarification, acidic deinking processes, high-salt food processing, textile and pulp industries, and for biofuel production from seaweeds.

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“…strain DY3 shows very similar optimal temperature and thermostability (64). However, Cell5.1_3 is active over a broad pH range, from 5 to 8, and is stable at pH values from 4 to 10 (it is still active after a 24-hour preincubation in this pH range), which is not the case for the cold-active CelX (64). What is more, other metagenome-derived GH5 cellulases show stability only at acidic (4 to 6.6 [59]) or alkaline (6 to 10 [55]) pH.…”

Section: Discussionmentioning

confidence: 96%

“…A cold-active cellulase (CelX) identified in Pseudoalteromonas sp. strain DY3 shows very similar optimal temperature and thermostability (64). However, Cell5.1_3 is active over a broad pH range, from 5 to 8, and is stable at pH values from 4 to 10 (it is still active after a 24-hour preincubation in this pH range), which is not the case for the cold-active CelX (64).…”

Section: Discussionmentioning

confidence: 97%

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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Characterization and gene cloning of a cold-active cellulase from a deep-sea psychrotrophic bacterium Pseudoalteromonas sp. DY3

Cited by 65 publications

References 15 publications

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

Culturable heterotrophic bacteria from Potter Cove, Antarctica, and their hydrolytic enzymes production

A cold-active acidophilic endoglucanase of Paenibacillus sp. Y2 isolated from soil in an alpine region

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

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