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. 2015 Mar;90(3):573-581.
doi: 10.1002/jctb.4589. Epub 2014 Dec 8.

Application of a new xylanase activity from Bacillus amyloliquefaciens XR44A in brewer's spent grain saccharification

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Application of a new xylanase activity from Bacillus amyloliquefaciens XR44A in brewer's spent grain saccharification

Antonella Amore et al. J Chem Technol Biotechnol. 2015 Mar.

Abstract

Background: Cellulases and xylanases are the key enzymes involved in the conversion of lignocelluloses into fermentable sugars. Western Ghat region (India) has been recognized as an active hot spot for the isolation of new microorganisms. The aim of this work was to isolate new microorganisms producing cellulases and xylanases to be applied in brewer's spent grain saccharification.

Results: 93 microorganisms were isolated from Western Ghat and screened for the production of cellulase and xylanase activities. Fourteen cellulolytic and seven xylanolytic microorganisms were further screened in liquid culture. Particular attention was focused on the new isolate Bacillus amyloliquefaciens XR44A, producing xylanase activity up to 10.5 U mL-1. A novel endo-1,4-beta xylanase was identified combining zymography and proteomics and recognized as the main enzyme responsible for B. amyloliquefaciens XR44A xylanase activity. The new xylanase activity was partially characterized and its application in saccharification of brewer's spent grain, pretreated by aqueous ammonia soaking, was investigated.

Conclusion: The culture supernatant of B. amyloliquefaciens XR44A with xylanase activity allowed a recovery of around 43% xylose during brewer's spent grain saccharification, similar to the value obtained with a commercial xylanase from Trichoderma viride, and a maximum arabinose yield of 92%, around 2-fold higher than that achieved with the commercial xylanase. © 2014 The Authors. Journal of Chemical Technology & Biotechnology published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

Keywords: Bacillus; brewer's spent grain; saccharification; xylanase.

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Figures

Figure 1
Figure 1
Screening of cellulolytic (A) and xylanolytic (B) strains in liquid medium.
Figure 2
Figure 2
Detection of xylanase activity produced by XR44A after SDS-PAGE. Lane A: XR44A (0.25 U total xylanase activity); Lane B: XR44A (10 γ of total protein loaded); Lane C: Markers.
Figure 3
Figure 3
Optimum pH (A) and temperature (B) of xylanase activity produced by B. amyloliquefaciens XR44A.

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