Ontology highlight
ABSTRACT:
SUBMITTER: Wang X
PROVIDER: S-EPMC7194205 | biostudies-literature | 2020 Mar
REPOSITORIES: biostudies-literature
Wang Xinye X Jing Xiaoran X Deng Yi Y Nie Yao Y Xu Fei F Xu Yan Y Zhao Yi-Lei YL Hunt John F JF Montelione Gaetano T GT Szyperski Thomas T
FEBS letters 20191113 5
Pullulanases are well-known debranching enzymes hydrolyzing α-1,6-glycosidic linkages. To date, engineering of pullulanase is mainly focused on catalytic pocket or domain tailoring based on structure/sequence information. Saturation mutagenesis-involved directed evolution is, however, limited by the low number of mutational sites compatible with combinatorial libraries of feasible size. Using Bacillus naganoensis pullulanase as a target protein, here we introduce the 'evolutionary coupling satur ...[more]