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Xylan deterioration approach: Purification and catalytic behavior optimization of a novel β-1,4-d-xylanohydrolase from KIBGE-IB29. | LitMetric

AI Article Synopsis

  • The β-1,4-d-xylanohydrolase enzyme from KIBGE-IB29 was purified with a 52% recovery yield and displayed optimal activity at pH 7.0 and 50°C.
  • It retained considerable activity in various pH levels (pH 4.0 to 9.0) and temperatures (40°C to 70°C), showcasing significant stability and performance.
  • The enzyme's activity increased significantly with additives like ethanol and surfactants, suggesting its potential applications in the textile and food industries due to its remarkable stability over time.

Article Abstract

The β-1,4-d-xylanohydrolase is an industry valuable catalytic protein and used to synthesize xylooligosaccharides and xylose. In the current study, β-1,4-d-xylanohydrolase from KIBGE-IB29 was partially purified up to 9.5-fold with a recovery yield of 52%. It exhibited optimal catalytic activity at pH-7.0 and 50 °C within 5 min. Almost 50% activity retained at pH-4.0 to 9.0 however, 70% activity observed within the range of 40 °C to 70 °C. The β-1,4-d-xylanohydrolase showed a significant hydrolytic pattern with 48.7 kDa molecular mass. It was found that the enzymatic activity improved up to 160% with 1.0 mM ethanol. Moreover, the activity of enzyme drastically increased up to 2.3 and 1.5 fold when incubated with Tween 80 and Triton X-100 (1.0 mM), respectively. The β-1,4-d-xylanohydrolase also retained 72% activity at -80 °C after 180 days. Such a remarkable biochemical properties of β-1,4-d-xylanohydrolase make it possible to forecast its potential use in textile and food industries.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6312829PMC
http://dx.doi.org/10.1016/j.btre.2018.e00299DOI Listing

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