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Generating bifunctional fusion enzymes composed of heat-active endoglucanase (Cel5A) and endoxylanase (XylT)
Publikationstyp
Journal Article
Date Issued
2015-01-17
Sprache
English
Author(s)
Institut
TORE-URI
Journal
Volume
37
Issue
1
Start Page
139
End Page
145
Citation
Biotechnology Letters 1 (37): 139-145 (2015-01-17)
Publisher DOI
Scopus ID
PubMed ID
25214221
Bifunctional enzyme constructs were generated comprising two genes encoding heat-active endoglucanase (cel5A) and endoxylanase (xylT). The fused proteins Cel5A–XylT and XylT–Cel5A were active on both β-glucan and beechwood xylan. An improvement in endoglucanase and endoxylanase catalytic activities was observed. The specific activity of the fusion towards xylan was significantly raised when compared to XylT. The fusion constructs were active from 40 to 100 °C for endoglucanase and from 40 to 90 °C for endoxylanase, but the temperature optima were lowered from 90 to 80 °C for the endoglucanase and from 80 to 70 °C for the endoxylanase. XylT in the construct XylT–Cel5A was less stable at higher temperatures compared to Cel5A–XylT. Due to the enzymatic performance, these fusion enzymes are attractive candidates for applications in biorefineries based on plant waste.
Subjects
Bifunctional
Cellulase
End-to-end gene fusion
Extremophiles
Thermozymes
Xylanase