A novel cold-active GH8 xylanase from cellulolytic myxobacterium and its application in food industry

Xu Li, Lei Zhang, Zhitong Jiang, Lin Liu, Jihong Wang, Lingli Zhong, Tao Yang, Qin Zhou, Weiliang Dong, Jie Zhou, Xianfeng Ye, Zhoukun Li, Yan Huang, Zhongli Cui

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Although xylanase have a wide range of applications, cold-active xylanases have received less attention. In this study, a novel glycoside hydrolase family 8 (GH8) xylanase from Sorangium cellulosum with high activity at low temperatures was identified. The recombinant xylanase (XynSc8) was most active at 50 °C, demonstrating 20% of its maximum activity and strict substrate specificity towards beechwood and corncob xylan at 4 °C with Vmax values of 968.65 and 1521.13 μmol/mg/min, respectively. Mesophilic XynSc8 was active at a broad range of pH and hydrolyzed beechwood and corncob xylan into xylooligosaccharides (XOS) with degree of polymerization greater than 3. Moreover, incorporation of XynSc8 (0.05–0.2 mg/kg flour) provided remarkable improvement (28–30%) in bread specific volume and textural characteristics of bread compared to commercial xylanase. This is the first report on a novel cold-adapted GH8 xylanase from myxobacteria, suggesting that XynSc8 may be a promising candidate suitable for bread making.

Original languageEnglish
Article number133463
JournalFood Chemistry
Volume393
DOIs
StatePublished - 1 Nov 2022

Keywords

  • Bread making
  • Cold-adaptation
  • Sorangium cellulosum
  • Xylanase
  • Xylooligosaccharides

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