Table 6.

The yield and structure of the products of transglycosylation reactions catalyzed by the recombinant wild α-PsGal and its mutant C494N based on NMR data.

Enzyme	Substrate	T (°C)	Substrate Conversion (%)	Structure of the Hydrolysis and Transglycosylation Products		Yield of Products (%)
Wild	Gal-α(1→6)-Glcα,β	20	88.5	Gal	1	45.627.35.50.6
				Glc	2
				Gal-α(1→6)-Galα,β	3
				Gal-α(1→4)-Galα,β	4
Wild	Gal-α(1→6)-Glcα,β	8	90.2	Gal	1	46.035.07.81.4
				Glc	2
				Gal-α(1→6)-Galα,β	3
				Gal-α(1→4)-Galα,β	4
Wild	pNP-α-Gal	20	67.2	Gal	1	21.58.03.01.21.2
				Gal-α(1→6)-Gal-α-pNP	6
				Gal-α(1→6)-Galα,β	3
				Gal-α(1→4)-Galα,β	4
				Gal-α(1→3)-Gal-α-pNP	7
Wild	pNP-α-Gal	8	15.9	Gal	1	9.84.11.20.78<1
				Gal-α(1→6)-Gal-α-pNP	6
				Gal-α(1→6)-Galα,β	3
				Gal-α(1→4)-Galα,β	4
				Gal-α(1→3)-Gal-α-pNP	7
Wild	Gal-α(1→6)-Glcα,β + pNP-α-Gal	20	32.0	Gal	1	30.09.01.60.8
				Gal-α(1→6)-Gal-α-pNP	6
				Gal-α(1→4)-Galα,β	4
				Gal-α(1→6)-Galα,β	3
C494N	pNP-α-Gal	8	19.0	Gal	1	5.02.82.01.2
				Gal-α(1→6)-Galα,β	3
				Gal-α(1→6)-Gal-α-pNP	6
				Gal-α(1→4)-Galα,β	4