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Table 4 Comparison of the kinetic constants of BGL-3 with other laminarin-degradative enzymes, using laminarin as substrate

From: The β-glucosidase secreted by Talaromyces amestolkiae under carbon starvation: a versatile catalyst for biofuel production from plant and algal biomass

Organism Enzyme K m k cat k cat /K m References
Podospora anserina PaGluc131A 4.1a 51.9a 12.6 [35]
Pseudoalteromonas sp. Strain BB1 ExoP 0.7 204.9 290.9 [36]
Talaromyces emersonii Exo-1,3-β-glucanase 1.6 29.5 17.8 [37]
Paddy soil microbial metagenome Umcel9y-1 47.3 127.5 2.6 [38]
Aspergillus fumigatus 1,3-β-glucanase 0.2 56.9a 219.1a [30]
Vibrio campbellii LamN 4.0 0.8 0.1 [33]
Barley -d-glucan ExoII 0.1 28.0 230.0 [39]
ExoI 0.1 73.0 740.0 [39]
T. amestolkiae BGL-3 BGL-3b 1.2 253.9 211.5 This work
BGL-3c 1.1 247.9 225.3 This work
  1. a Calculated from data provided in the original article
  2. b Substrate: laminarin from L. digitata
  3. c Substrate: laminarin from L. hyperborea