Engineering a Disulfide Bond in the Lid Hinge Region of Rhizopus chinensis Lipase: Increased Thermostability and Altered Acyl Chain Length Specificity

@inproceedings{Yu2012EngineeringAD,
  title={Engineering a Disulfide Bond in the Lid Hinge Region of Rhizopus chinensis Lipase: Increased Thermostability and Altered Acyl Chain Length Specificity},
  author={Xiao-Wei Yu and Nian-Jiang Tan and Rong Xiao and Yan Xu},
  booktitle={PloS one},
  year={2012}
}
The key to enzyme function is the maintenance of an appropriate balance between molecular stability and structural flexibility. The lid domain which is very important for "interfacial activation" is the most flexible part in the lipase structure. In this work, rational design was applied to explore the relationship between lid rigidity and lipase activity by introducing a disulfide bond in the hinge region of the lid, in the hope of improving the thermostability of R. chinensis lipase through… CONTINUE READING

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References

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Showing 1-10 of 35 references

Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge

  • L Quang Anh Tuan, JC Joo, YJ Yoo, YH Kim
  • Biotechnol Bioeng
  • 2012
1 Excerpt

Protein engineering and discovery of lipases

  • R Kourist, H Brundiek, UT Bornscheuer
  • Eur J Lipid Sci Tech
  • 2010

Rhizopus chinensis lipase: Gene cloning, expression in Pichia pastoris and properties

  • XW Yu, LL Wang, Y Xu
  • J Mol Catal B-Enzym
  • 2009

Biodiesel production catalyzed by wholecell lipase from Rhizopus chinensis

  • Q He, Y Xu, Y Teng, D Wang
  • Chinese Journal of Catalysis
  • 2008
1 Excerpt

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