Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering

Eitemau Tebyg

• Improvement of the thermostability and catalytic efficiency of a highly active β-glucanase from Talaromyces leycettanus JCM12802 by optimizing residual charge–charge interactions
  gan: You, Shuai, et al.
  Cyhoeddwyd: (2016)
• A Swollenin From Talaromyces leycettanus JCM12802 Enhances Cellulase Hydrolysis Toward Various Substrates
  gan: Zhang, Honghai, et al.
  Cyhoeddwyd: (2021)
• Improvement of the catalytic efficiency of a hyperthermophilic xylanase from Bispora sp. MEY-1
  gan: Wang, Xiaoyu, et al.
  Cyhoeddwyd: (2017)
• A Novel Thermostable GH3 β-Glucosidase from Talaromyce leycettanus with Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability
  gan: Li, Xinxin, et al.
  Cyhoeddwyd: (2018)
• Synergistic effect of acetyl xylan esterase from Talaromyces leycettanus JCM12802 and xylanase from Neocallimastix patriciarum achieved by introducing carbohydrate-binding module-1
  gan: Zhang, Yueqi, et al.
  Cyhoeddwyd: (2019)