2. Academic Validation
  3. Hydrolytic properties of a hybrid xylanase and its parents

Hydrolytic properties of a hybrid xylanase and its parents

  • Appl Biochem Biotechnol. 2009 Mar;152(3):428-39. doi: 10.1007/s12010-008-8316-y.
Jian-Yi Sun 1,  Ming-Qi Liu,  Xiao-Yan Weng
Affiliations

Affiliation

  • 1 Microbiology Division, Key Laboratory of Molecular Animal Nutrition, Ministry of Education, College of Animal Science, Zhejiang University, Hangzhou 310029, People's Republic of China.
PMID: 18688581 DOI: 10.1007/s12010-008-8316-y
Abstract

The hydrolytic properties of a hybrid xylanase (ATx) and its parents (reAnxA and reTfxA) were studied using xylans and xylooligosaccharides as substrates. Analysis of reaction mixtures by high-performance liquid chromatograph revealed that xylotriose (X3) was the main product released from birchwood xylan and wheat bran insoluble xylan by ATx and reAnxA, respectively. Xylobiose (X2) was the main product separately released from birchwood xylan and wheat bran insoluble xylan by reTfxA. Xylotetraose (X4), xylopentaose (X5), and xylohexaose (X6) could be hydrolyzed by ATx, which showed no activity on X2 and X3. Therefore, X4 might be the minimum oligomer hydrolyzed by ATx. X2-X6 could be hydrolyzed by reAnxA and reTfxA, respectively. All of ATx, reAnxA, and reTfxA showed transglycosylation activity.

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