Biochemical characterization of a novel xylanase from Paenibacillus barengoltzii and its application in xylooligosaccharides production from corncobs. (30th October 2018)

• Record Type: Journal Article
• Authors: Liu, Xueqiang; Liu, Yu; Jiang, Zhengqiang; Liu, Haijie; Yang, Shaoqing; Yan, Qiaojuan
• Is Part Of: Food chemistry. Volume 264(2018)
• Page Start: 310
• Page End: 318
• Publication Date: 2018-10-30
• Subjects: Xylose (PubChem CID: 135191) -- Xylobiose (PubChem CID: 439538) -- Xylotriose (PubChem CID: 10201852) -- Xylotetraose (PubChem CID: 10230811) -- Xylopentaose (PubChem CID: 10146542) -- Xylan from birchwood (PubChem CID: 50909243) -- PNP-β-d-xylopyranoside (PubChem CID: 91509); Xylanase -- Paenibacillus barengoltzii -- Characterization -- Steam explosion -- Acidic electrolyzed water -- Xylooligosaccharide; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2018.05.023
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: A novel xylanase gene from Paenibacillus barengoltzii was cloned and expressed. The recombinant xylanase was most active at pH 6.5 and 60 °C. The enzyme exhibited strict substrate specificity towards various xylans. The enzyme converted corncobs to xylooligosaccharide with the highest yield of 75%. Abstract: A novel xylanase gene ( PbXyn10A ) from Paenibacillus barengoltzii was cloned and expressed in Escherichia coli . PbXyn10A had an open reading frame of 3, 063 bp, and its deduced amino acid sequence shared the highest identity of 72% with a xylanase from Paenibacillus curdlanolyticus. The recombinant xylanase ( Pb Xyn10A) was purified and biochemically characterized. Pb Xyn10A was most active at pH 6.5 and 60 °C, respectively. It exhibited strict substrate specificity towards birchwood xylan, beechwood xylan and oat-spelt xylan, with K m values of 2.19, 2.04 and 2.51 mg/mL, respectively. The enzyme hydrolyzed xylan to yield mainly xylooligosaccharides (XOS) with degree of polymerization 2–4. A new strategy for XOS production from corncobs pretreated by steam explosion using acidic electrolyzed water, followed by enzymatic hydrolysis was developed. The highest XOS yield of 75% (based on xylan in raw corncobs) was achieved. This is the first report on a xylanase from Paenibacillus barengoltzii .