Enhanced expression and activity yields of Clostridium thermocellum xylanases without non-catalytic domains

Sajjad, Muhammad; Khan, Muhammad Imran; Nadeem, Muhammad Shahid; Ahmad, Sajjad; Imran, Ali; Akhtar, Muhammad

doi:10.1016/j.jbiotec.2009.10.013

Cited by 30 publications

(18 citation statements)

References 18 publications

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“…4). We have reported previously that the presence of binding domain at N-terminus, as in XynC-BC only 20% of the activity was lost when incubated at 70 • C for 120 min (Sajjad et al, 2010). Shin et al, 2002 also showed that transposition of xylan binding domain of XynX showed little effect on substrate binding but led to lower thermostability, when the binding domain was shifted from the native N-to C-terminal.…”

Section: Enzyme Characteristicsmentioning

confidence: 88%

“…In a previous study we reported enhanced expression of truncated derivatives of XynC and XynZ (Sajjad et al, 2010). The presence of family 22 carbohydrate binding domain was found to enhance thermostability of XynC.…”

Section: Introductionmentioning

confidence: 87%

“…Therefore this factor was likely to have similar effect on the expression of the two variants. Previously, we have reported that XynC having binding domain at the N-terminal (XynC-BC) and the one without a binding domain (XynC-C) when expressed in E. coli showed similar level of specific activities in the cell lysate supernatant when assayed against solublized birchwood xylan (Sajjad et al, 2010). In this study, activities of these two enzymes and the two newly produced variants, i.e., XynC-CB and XynC-BCB were compared against the insoluble substrates.…”

Section: Xylanase Expression and Activity Yieldsmentioning

confidence: 99%

“…For determining pH stability, the enzyme sample was incubated at room temperature (30 • C) at pH 3-10, for 120 min and the residual activity was assayed using solublized birchwood xylan, obtained as described previously (Sajjad et al, 2010).…”

Section: Effect Of Ph and Temperature On Stabilitymentioning

confidence: 99%

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Influence of transposition and insertion of additional binding domain on expression and characteristics of xylanase C of Clostridium thermocellum

Khan

Sajjad

Imran

et al. 2010

Journal of Biotechnology

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Section: Enzyme Characteristicsmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 87%

Section: Xylanase Expression and Activity Yieldsmentioning

confidence: 99%

Section: Effect Of Ph and Temperature On Stabilitymentioning

confidence: 99%

See 2 more Smart Citations

Influence of transposition and insertion of additional binding domain on expression and characteristics of xylanase C of Clostridium thermocellum

Khan

Sajjad

Imran

et al. 2010

Journal of Biotechnology

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“…For all cases, single enzymes or combination of enzymes, the enzyme loading was kept at 100 nM. domain of XynZ, since it has higher activity against insoluble birchwood xylan than that of intact enzyme [25]. Conversely, Xyn11A has a special CBM, so-called XBM, that can bind to both cellulose and xylan, thus increasing the interactions between xylan and enzymes [26].…”

Section: Calculation Of the Degree Of Synergy (Ds)mentioning

confidence: 99%

Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase

Jia

Budinova

Takasugi

et al. 2016

Biochemical Engineering Journal

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Effective degradation of hemicellulose is of utmost importance in a wide variety of applications in bioindustry. Five endoxylanases from different glycoside hydrolase families and microorganisms were tested with an arabinofuranosidase, Araf51A, for the hydrolysis of insoluble wheat arabinoxylan, which is a structural component of hemicellulose. The optimized combination was XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increased with the increase of Araf51A proportion in the enzyme mixture. Afterwards, selected enzymes were immobilized on commercial magnetic nanoparticles through covalent bonding. Both free and immobilized enzymes showed a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes was retained. A 5.5-fold increase in the production of sugars was obtained with a mixture of enzymes immobilized after 10 cycles in total compared with free enzymes. Importantly, a sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan was demonstrated.

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Heat‐ and Alkaline‐Stable Xylanases: Application, Protein Structure and Engineering

Chen

Huang³

et al. 2015

ChemBioEng Reviews

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Xylan is the most abundant hemicellulosic component, and its degradation is the major step in a wide variety of industrial processes. Xylanases, which are capable of randomly hydrolyzing the β‐1,4‐xylosidic linkages, constitute the key enzymes in xylan decomposition. As xylanases hold a high economic potential in the marketplace, great efforts have been made in search of suitable candidates for the development into commercial products with better performances such as higher specific activity, better thermostability, higher operating temperatures, and a better pH profile. To achieve these goals, the three‐dimensional structural information of xylanases with the extremophilic properties is of pivotal importance. In this review, the current knowledge about heat‐ and alkaline‐stable xylanase structures is summarized, including protein engineering studies and focusing on the glycoside hydrolase families 10 and 11 enzymes. These structures pave the way to understanding the catalytic mechanisms of xylanases and provide an important engineering basis for their industrial applications.

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Enhanced expression and activity yields of Clostridium thermocellum xylanases without non-catalytic domains

Cited by 30 publications

References 18 publications

Influence of transposition and insertion of additional binding domain on expression and characteristics of xylanase C of Clostridium thermocellum

Influence of transposition and insertion of additional binding domain on expression and characteristics of xylanase C of Clostridium thermocellum

Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase

Heat‐ and Alkaline‐Stable Xylanases: Application, Protein Structure and Engineering

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