Abstract：
:Industrial application of Caldicellulosiruptor saccharolyticus cellobiose 2-epimerase (CsCE) for lactulose synthesis is limited by low enzyme activity and formation of epilactose as by-product. After four sequential rounds of random mutagenesis and screening, an optimal mutant G4-C5 was obtained. Compared with wild type (WT) enzyme, mutant G4-C5 demonstrated 2.8- and 3.0-fold increases in specific activity and kcat/Km for lactulose production, respectively, without compromising thermostability. DNA sequencing of mutant G4-C5 revealed five amino acid substitutions, namely, R5M, I52V, A12S, K328I and F231L, which were located on the protein surface, except for the mutation I52V. The yield of lactulose catalyzed by mutant G4-C5 increased to approximately 76% with no obvious epilactose detected, indicating that mutant G4-C5 was more suitable for lactulose production than the WT enzyme.
journal_name
Food Chemjournal_title
Food chemistryauthors
Shen Q,Zhang Y,Yang R,Pan S,Dong J,Fan Y,Han Ldoi
10.1016/j.foodchem.2016.02.067subject
Has Abstractpub_date
2016-09-15 00:00:00pages
60-7eissn
0308-8146issn
1873-7072pii
S0308-8146(16)30228-Xjournal_volume
207pub_type
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