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

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

Organism	Enzyme	K _m	k _cat	k _cat /K _m	References
Podospora anserina	PaGluc131A	4.1^a	51.9^a	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	56.9^a	219.1^a	[30]
Vibrio campbellii	LamN	4.0	0.8	0.1	[33]
Barley -d-glucan	ExoII	0.1	28.0	230.0	[39]
Barley -d-glucan	ExoI	0.1	73.0	740.0	[39]
T. amestolkiae BGL-3	BGL-3^b	1.2	253.9	211.5	This work
T. amestolkiae BGL-3	BGL-3^c	1.1	247.9	225.3	This work

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