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Table 1 Enzyme activity in culture supernatant and specific activity for P. pastoris-expressed wild-type and mutant D2-BGL

From: Improvements of the productivity and saccharification efficiency of the cellulolytic β-glucosidase D2-BGL in Pichia pastoris via directed evolution

Pichia pastoris strain Mutation Activitya, b (U/mL) Relative activityc (%) Specific activityb (U/mg)
WT D2   2.31 ± 0.20 100 ± 9 213 ± 8
Mut A D358G + S496P 2.24 ± 0.04 97 ± 2 218 ± 1
D358G D358G 1.77 ± 0.21 77 ± 9 164 ± 10
S496P S496P 1.94 ± 0.12 84 ± 5 182 ± 8
Mut B D224G + S592T 4.29 ± 0.42 186 ± 18 229 ± 19
D224G D224G 4.08 ± 0.36 177 ± 16 202 ± 19
S592T S592T 1.72 ± 0.51 75 ± 22 195 ± 13
Mut C F256M + Y260D 4.09 ± 0.52 177 ± 23 253 ± 29
F256M F256M 3.01 ± 0.59 130 ± 25 301 ± 26
Y260D Y260D 1.92 ± 0.38 83 ± 17 189 ± 11
D224G F256M D224G + F256M 5.70 ± 0.26 247 ± 11 236 ± 14
D224G Y260D D224G + Y260D 4.63 ± 0.70 200 ± 30 192 ± 4
Mut M D224G + F256M + Y260D 7.5 ± 0.75 325 ± 33 261 ± 23
  1. aEnzyme activity is measured with a 3-day culture supernatant
  2. bEnzyme activity and specific activity are determined at 10 mM cellobiose
  3. cRelative activity is determined based on the enzyme activity of WT D2