Biochemical characteristics and molecular mechanism of an exo-type alginate lyase VxAly7D and its use for the preparation of unsaturated monosaccharides

Table 3 Comparison of recombinant VxAly7D with other alginate lyases

Enzyme	Source	Family	Specific activity	Optimal temperature	Percent of the maximal activity at 20 °C (%)	Substrate specificity	Products (DP)	Action mode	References
VxAly7D	Vibrio xiamenensis QY104	PL7	462.4 U/mg	30	90	Sodium alginate ≈ polyM > polyG	1–3	Exo-type	In this study
AlyA5	Zobellia galactanivorans Dsij^T	PL7	449.3 U/mg	30	No data	PolyG > polyMG > polyM	1–2	Exo-type	[18]
AlyPM	Pseudoalteromonas sp. SM0524	PL7	No data	30	52	PolyM > sodium alginate > polyG	2–3	Endo-type	[16]
Algb	Vibrio sp. W13	PL7	457 U/mg	30	80	Sodium alginate ≈ polyMG > polyG > polyM	2–5	Endo-type	[62]
AlyA1_PL7	Zobellia galactanivorans Dsij^T	PL7	No data	30	82	PolyG > polyM	2–4	Endo-type	[18]
TsAly6A	Thalassomonas sp. LD5	PL6	189 U/mg	35	73.1	PolyG ≈ alginate > polyM	2–3	Endo-type	[14]
AlyGC	Glaciecola chathamensis S18K6^T	PL6	170 U/mg	30	82.5	PolyG > polyM > sodium alginate	1	Exo-type	[15]
AkAly30	Aplysia kurodai	PL14	210 U/mg	55	20	PolyM > alginate > polyMG > polyG	1–3	Endo- and exo-type	[63, 64]
A1-IV	Sphingomonas sp. A1	PL15	7.5 U/mg^a	37	No data	polyM ≈ polyG	1	Exo-type	[65]
AlgL17	Microbulbifer sp. ALW1	PL17	No data	35	≤ 65	PolyM > alginate > polyG	1–4	Exo-type	[56]

All of the activity was defined by measuring the increase in absorbance at 235 nm
^aThe activity of A1-IV was calculated according to the method described by Fu et al. [66]

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