2023
DOI: 10.1016/j.renene.2023.02.043
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Efficient fermentable sugar production from mulberry branch based on a rational design of GH10 xylanase with improved thermal stability

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Cited by 10 publications
(2 citation statements)
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“…Enzymes can be expressed naturally or heterologously, depending on where the coding sequence has been located, to later be inserted into prokaryotes and ascomycetes [ 106 , 107 ]. Based on the above, an isolated, efficient, and abundant production is sought to reduce costs and time in results, for which mutation processes have also been generated, where the change of amino acids in the active site sometimes achieves a greater catalytic reaction speed, thermal stability, and tolerance to salinity, which allows them to continue active in catabolism or anabolism depending on the process to be carried out [ 108 , 109 , 110 ].…”
Section: Recent Trendsmentioning
confidence: 99%
“…Enzymes can be expressed naturally or heterologously, depending on where the coding sequence has been located, to later be inserted into prokaryotes and ascomycetes [ 106 , 107 ]. Based on the above, an isolated, efficient, and abundant production is sought to reduce costs and time in results, for which mutation processes have also been generated, where the change of amino acids in the active site sometimes achieves a greater catalytic reaction speed, thermal stability, and tolerance to salinity, which allows them to continue active in catabolism or anabolism depending on the process to be carried out [ 108 , 109 , 110 ].…”
Section: Recent Trendsmentioning
confidence: 99%
“…Based on protein structure analysis, mutations at speci c amino acid sites have been demonstrated to signi cantly improve enzyme stability (25). For instance, the rational design of Xylanase Hwxyl10A from Hortaea werneckii led to a 17-fold improvement in thermostability at 50°C (3). The active pocket is a critical site for enzyme catalysis, and although the active site is highly conserved, changes in amino acids near the active site can also have a signi cant impact on enzyme activity and function, even if this relationship has not been reported (30).…”
Section: Introductionmentioning
confidence: 99%