A novel endo-β-1, 4-xylanase GH30 from Dickeya dadantii DCE-01: Clone, expression, characterization, and ramie biological degumming function. Issue 4 (February 2019)

• Record Type: Journal Article
• Authors: Wang, Ruijun; Liu, Zhengchu; Cheng, Lifeng; Duan, Shengwen; Feng, Xiangyuan; Zheng, Ke; Cheng, Yi; Zeng, Jie
• Is Part Of: Textile research journal. Volume 89:Issue 4(2019)
• Page Start: 463
• Page End: 472
• Publication Date: 2019-02
• Subjects: Dickeya dadantii DCE-01 -- xylanase -- prokaryotic expression -- ramie biological degumming; Textile industry -- Periodicals; Textile fabrics -- Periodicals; Textile research -- Periodicals; Textiles et tissus -- Industrie et commerce -- Périodiques; Textiles et tissus -- Périodiques; Textiles et tissus -- Recherche -- Périodiques; Electronic journals; 677.005
• DOI: 10.1177/0040517517748511
• Languages: English
• ISSNs: 0040-5175

Abstract

Xylanase plays an important role in the hydrolysis of hemicellulose and has gained much attention in the field of biological degumming. The research for xylanases with cellulase-free and high activity for biological degumming has intensified in recent years. In the present research, heterologous expression of a novel endo-β-1, 4-xylanase (GH30) from Dickeya dadantii DCE-01 in Escherichia coli BL21 (DE3) was reported. Biochemical characterization of the enzyme and a potential application in ramie biological degumming was discussed. The results showed that the xylanase gene consists of 1251 nucleotides, belonging to glycoside hydrolase family 30 (GH30). The optimal activity of the xylanase was observed at 50℃ and a pH value of 6.4. The Km and V max values for beechwood xylan were 14.25 mg/mL and 296.6 μmol/mg, respectively. The catalytic activity was enhanced by addition of 1 mM Cu 2+, Ca 2+, Mg 2+, and K + . The recombinant enzyme was specific for xylan substrates. The enzyme exhibited hydrolytic activity toward ramie hemicellulose. The recombinant xylanase could be effectively applied to ramie degumming.