Production of xylose through enzymatic hydrolysis of glucuronoarabinoxylan from brewers’ spent grain

Abstract

Xylose is an abundant bioresource for obtaining diverse chemicals and added-value products. The production of xylose from green alternatives like enzymatic hydrolysis is an important step in a biorefinery context. This research evaluated the synergism among four classes of hydrolytic purified enzymes—endo-1,4-β-xylanase, α-l-arabinofuranosidase, β-xylosidase, and α-d-glucuronidase—over hydrolysis of glucuronoarabinoxylan (GAX) obtained from brewers’ spent grain (BSG) after alkaline extraction and ethanol precipitation. First, monosaccharides, uronic acids and glycosidic-linkages of alkaline extracted GAX fraction from BSG were characterized, after that different strategies based on the addition of one or two families of enzymes—endo-1,4-β-xylanase (GH10 and GH11) and α-l-arabinofuranosidase (GH43 and GH51)—cooperating with one β-xylosidase (GH43) and one α-d-glucuronidase (GH67) into enzymatic hydrolysis were assessed to obtain the best yield of xylose. The xylose release was monitored over time in the first 90 min and after a prolonged reaction up to 48 h of reaction. The highest yield of xylose was 63.6% (48 h, 40 ℃, pH 5.5), using a mixture of all enzymes devoid of α-l-arabinofuranosidase (GH43) family. These results highlight the importance of GH51 arabinofuranosidase debranching enzyme to allow a higher cleavage of the xylan backbone of GAX from BSG and their synergy with 2 endo-1,4-β-xylanase (GH10 and GH11), one β-xylosidase (GH43) and the inclusion of one α-d-glucuronidase (GH67) in the reaction system. Therefore, this study provides an environmentally friendly process to produce xylose from BSG through utilization of enzymes as catalysts. Graphical Abstract

Monitoring corn stover processing by the fungus Ustilago maydis

“…GAX, the primary matrix polysaccharide in grasses, is characterized by a highly O-acetylated linear β-1,4-linked D-xylopyranose backbone which can be further decorated with pentose, hexose, and (methyl)uronic or hydroxycinnamic acid sidechains (13). This structural heterogeneity hinders enzymatic degradation, and multiple enzymes with speci c substrate recognition and cleavage capabilities are needed to e ciently convert GAX (14,15). Lignin is an aromatic heteropolymer consisting mainly of guaiacyl, syringyl and/or phydroxyphenyl monolignol subunits.…”