Isolation and characterization of a non-specific endoglucanase from a metagenomic library of goat rumen

Cheng, Jianbo; Huang, Shuai; Jiang, Hua; Zhang, Yunhai; Li, Lvmu; Wang, Juhua; Fan, Caiyun

doi:10.1007/s11274-015-1957-4

Cited by 28 publications

(11 citation statements)

References 20 publications

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“…As the AA sequence of CbGH5 homologues is highly conserved in Chryseobacterium genus, they might potentially be interesting objects for mining cellulase or bifunctional cellulase–xylanase candidates. Bifunctional cellulase–xylanase activities were previously reported in GH7 (Nakazawa et al ., ; Karnaouri et al ., ; Pellegrini et al ., ), GH10 (Ding et al ., ; Hess et al ., ) and GH61 (Jagtap et al ., ) as well as in GH5_2 (Ghatge et al ., ), GH5_4 (Chang et al ., ; Hess et al ., ; Rashamuse et al ., ; Cheng et al ., ; Rattu et al ., ) and GH5_25 (Yuan et al ., ) (Table ), while CbGH5 is the first example in GH5_46. To date, CbGH5 and a metagenome‐derived protein 421339_68070/TW‐2 (GenBank accession number: ) (Hess et al ., ) are the only two glycoside hydrolases of GH5_46 that have been characterized.…”

Section: Discussionmentioning

confidence: 98%

“…The overexpressed and purified CbGH5 showed maximum EG‐CMC and XYN‐bw activities at pH 9 and 8, respectively, which are both slightly alkalic. It differs from a number of cellulases and xylanases, whose optimum pH is usually acidic (Nakazawa et al ., ; Ghatge et al ., ; Jagtap et al ., ; Karnaouri et al ., ; Lafond et al ., ; Wang et al ., ; Cheng et al ., ; Pellegrini et al ., ). The enzyme is more stable at alkalic pH than acidic.…”

Section: Discussionmentioning

confidence: 99%

“…Accordingly, bifunctional enzymes possessing cellulase and xylanase activities could be more effective. In previous studies, bifunctional cellulase–xylanase enzymes with optimum temperatures around 50–65 °C were found in rumen microbial communities (Chang et al ., ; Rashamuse et al ., ; Cheng et al ., ), which are always rich sources of cellulolytic microbes and biomass‐degrading genes (Hess et al ., ).…”

Section: Introductionmentioning

confidence: 99%

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A bifunctional cellulase–xylanase of a new Chryseobacterium strain isolated from the dung of a straw‐fed cattle

Tan

Miao

Liu

et al. 2017

Microbial Biotechnology

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SummaryA new cellulolytic strain of Chryseobacterium genus was screened from the dung of a cattle fed with cereal straw. A putative cellulase gene (cbGH5) belonging to glycoside hydrolase family 5 subfamily 46 (GH5_46) was identified and cloned by degenerate PCR plus genome walking. The CbGH5 protein was overexpressed in Pichia pastoris, purified and characterized. It is the first bifunctional cellulase–xylanase reported in GH5_46 as well as in Chryseobacterium genus. The enzyme showed an endoglucanase activity on carboxymethylcellulose of 3237 μmol min−1 mg−1 at pH 9, 90 °C and a xylanase activity on birchwood xylan of 1793 μmol min−1 mg−1 at pH 8, 90 °C. The activity level and thermophilicity are in the front rank of all the known cellulases and xylanases. Core hydrophobicity had a positive effect on the thermophilicity of this enzyme. When similar quantity of enzymatic activity units was applied on the straws of wheat, rice, corn and oilseed rape, CbGH5 could obtain 3.5–5.0× glucose and 1.2–1.8× xylose than a mixed commercial cellulase plus xylanase of Novozymes. When applied on spent mushroom substrates made from the four straws, CbGH5 could obtain 9.2–15.7× glucose and 3.5–4.3× xylose than the mixed Novozymes cellulase+xylanase. The results suggest that CbGH5 could be a promising candidate for industrial lignocellulosic biomass conversion.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A bifunctional cellulase–xylanase of a new Chryseobacterium strain isolated from the dung of a straw‐fed cattle

Tan

Miao

Liu

et al. 2017

Microbial Biotechnology

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“…Nenhum dos íons metálicos avaliados nesse estudo exerceu influência significativa sobre a atividade das celulases. Zarafeta D et al (2016) (Cheng J et al, 2016); outras celulases podem ser inibidas por Ca 2+ , Mn 2+ e Co 2+ (Huang S et al, 2015); ou mesmo se mostrarem indiferentes quanto à presença de metais, como K, Zn 2+ , Mg 2+ e Na + (Asha BM et al, 2012).…”

Section: Discussionunclassified

Production of thermostable multiple enzymes from Bacillus amyloliquefaciens KUB29

Devaraj

Aathika

Periyasamy

et al. 2018

Natural Product Research

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A strain of Bacillus amyloliquefaciens KUB29 was identified by 16S ribosomal RNA sequencing (Genbank: MF772779.1). Production of thermostable protease, amylase and lipase were done by the isolated strain. The produced enzymes were partially purified by ammonium precipitation followed by dialysis process. Protease and lipase enzymes are effectively used in bio-oil extraction from proteinaceous sample followed by transesterification to produce methyl ester. Amylase enzyme is widely used in food and laundry industry. The produced enzymes are active at thermophilic condition of 55 °C. Use of these enzymes in biofuel production process will make the process cleaner and greener.

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“…The effects of metal ions on endoglucanases vary considerably. Most studies on the effects of the Cu 2+ ion have reported that it moderately or significantly inhibits purified endoglucanases (Li et al 2006;Fu et al 2010;Cheng et al 2016;Gupta et al 2017;Kanchanadumkerng et al 2017;Pimentel et al 2017;Segato et al 2017), but a few have been described enzyme activation by Cu…”

Section: Properties Of Eg-py2mentioning

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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Isolation and characterization of a non-specific endoglucanase from a metagenomic library of goat rumen

Cited by 28 publications

References 20 publications

A bifunctional cellulase–xylanase of a new Chryseobacterium strain isolated from the dung of a straw‐fed cattle

A bifunctional cellulase–xylanase of a new Chryseobacterium strain isolated from the dung of a straw‐fed cattle

Production of thermostable multiple enzymes from Bacillus amyloliquefaciens KUB29

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

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