2015
DOI: 10.1016/j.enzmictec.2015.06.013
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Protein engineering of Bacillus acidopullulyticus pullulanase for enhanced thermostability using in silico data driven rational design methods

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Cited by 52 publications
(19 citation statements)
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“…There are several works focused on improvement of the themostability of pullulanase derived from bacteria (Chen et al, 2015;Li et al, 2015;Chang et al, 2016;Wang et al, 2016). However, it is still lacking the understanding on the factor affecting the themostability of HvLD at the atomic level.…”
Section: Introductionmentioning
confidence: 99%
“…There are several works focused on improvement of the themostability of pullulanase derived from bacteria (Chen et al, 2015;Li et al, 2015;Chang et al, 2016;Wang et al, 2016). However, it is still lacking the understanding on the factor affecting the themostability of HvLD at the atomic level.…”
Section: Introductionmentioning
confidence: 99%
“…In addition to this, the mutants E631Y, E631F, and E631W also showed increased hydrophobic interactions after being mutated. The hydrophobic interaction is also one of the key factors in the thermal stability of protein, in fact the hydrophobic interactions were found to be marginally higher in thermophilic proteins than in mesophilic proteins (Chen et al, ; Guo et al, ). Thus, the thermostability improvement of mutants K573W, E631Y, E631F, and E631W may, at least partially, be due to the increase of these intramolecular interactions.…”
Section: Discussionmentioning
confidence: 99%
“…Manipulation on the thermal stability of enzymes is one of the basic topics in protein design and engineering. Conventionally, the thermal stability is optimized through iterative random residue mutations and in vitro screening 39 40 41 42 . Recently, numerous bioinformatics tools have been developed to facilitate the rational design on the protein stability using evolutionary information 43 .…”
Section: Discussionmentioning
confidence: 99%