title: [Screening for mutants with thermostabe lipase A from Burkholderia sp. ZYB002].
abstract: OBJECTIVE
  We improved the thermostability of LipA from Burkholderia cecapia ZYB002 by protein engineering technology to expand the application of lipase LipA.
  
  
  METHODS
  On the basis of B-factor value of lipase LipA, series of potential mutation hotspots were selected for iterative saturation mutagenesis and the corresponding small mutation gene libraries were then constructed to screen the hyperthermal variants.
  
  
  RESULTS
  From the above mutation libraries, we obtained a series of mutants whose enzyme half-life at 55 degrees C increased by 1.7 to 2.2-fold.
  
  
  CONCLUSIONS
  B-factor iterative test (B-FIT) is feasible to mutate thermostable strains.
authors.forename: Yanru
authors.initials: Y
authors.lastname: Liu
authors.forename: Liqing
authors.initials: L
authors.lastname: Qiu
authors.forename: Jianzhong
authors.initials: J
authors.lastname: Huang
authors.forename: Bingchun
authors.initials: B
authors.lastname: Zhao
authors.forename: Zuozhen
authors.initials: Z
authors.lastname: Wang
authors.forename: Xiaolan
authors.initials: X
authors.lastname: Zhu
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Gao
authors.forename: Zhengyu
authors.initials: Z
authors.lastname: Shu
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D019117:Burkholderia / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D004795:Enzyme Stability; D006358:Hot Temperature; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009154:Mutation; D015202:Protein Engineering; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D008049:Lipase