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Table 3 Comparison of recombinant VxAly7D with other alginate lyases

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

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 DsijT 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]
AlyA1PL7 Zobellia galactanivorans DsijT 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 S18K6T 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/mga 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]
  1. All of the activity was defined by measuring the increase in absorbance at 235 nm
  2. aThe activity of A1-IV was calculated according to the method described by Fu et al. [66]