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Table 1 Reported Tm(app) values for AA9 and AA10 LPMOs in the literature

From: A thermostable bacterial lytic polysaccharide monooxygenase with high operational stability in a wide temperature range

Enzyme (and additives)a

Tm(app) (°C)

pH (buffer)

Method

Domains

Reversible/irreversible folding

References

mgLPMO10-holo

83.0

6.0 (phosphate)

DSC

AA10-CBM2

Irreversible

This study

mgLPMO10-apo

73.0

6.0 (phosphate)

DSC

AA10-CBM2

Irreversible

This study

mgLPMO10CD-holo

76.0

6.0 (phosphate)

DSC

AA10

Irreversible

This study

ScLPMO10C-holo

64.1

6.0 (phosphate)

DSF

AA10-CBM2

ND

Jensen et al. [38]

SmLPMO10A-holo

71.2

6.0 (phosphate)

DSF

AA10

ND

Jensen et al. [38]

SmLPMO10A-holo

74.4

5.0 (acetate)

DSC

AA10

Reversible

Sugimoto et al. [45]

SmLPMO10A-apo

65.6

5.0 (acetate)

DSC

AA10

Reversible

Sugimoto et al. [45]

SmLPMO10A

70.3

8.0 (Tris–HCl)

ITF

AA10

ND

Vaaje-Kolstad et al. [46]

EfLPMO10A

72.0

8.0 (Tris–HCl)

ITF

AA10

ND

Vaaje-Kolstad et al. [46]

BaLPMO10A-holo

65.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

BaLPMO10A-apo

46.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

BaLPMO10A + EDTA

48.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

BaLPMO10A-Zn2+

52.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

BaLPMO10A-Ni2+

53.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

BaLPMO10A-Mn2+

46.0

5.0 (acetate)

DSF

AA10

ND

Hemsworth et al. [47]

TaLPMO9A-holo

74.3

7.0 (MOPS)

ITF

AA9

Reversible

Singh et al. [48]

TaLPMO9A-apo

65.2

7.0 (MOPS)

ITF

AA9

Reversible

Singh et al. [48]

TaLPMO9A-holo (deglycosylated)

67.9

7.0 (phosphate)

ITF

AA9

Reversible

Singh et al. [48]

MtLPMO9B

75.0b

7.0 (phosphate)

CD

AA9-CBM1

Irreversible

Frommhagen et al. [49]

MtLPMO9D

68.0b

7.0 (phosphate)

CD

AA9

Irreversible

Frommhagen et al. [49]

NcLPMO9C-holo

61.5

6.0 (phosphate)

DSF

AA9-CBM1

ND

Kracher et al. [44]c

NcLPMO9C-holo

44.0

4.0 (acetate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C-holo

34.7

4.0 (citrate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C-apo (+ EDTA)

52.7

6.0 (phosphate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C-holo + AscA

48.8

6.0 (phosphate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C-holo + xyloglucan

61.4

6.0 (phosphate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C-holo + xyloglucan + AscA

60.4

6.0 (phosphate)

DSF

AA9-CBM1

ND

Kracher et al. [44]

NcLPMO9C

63.0

6.0 (phosphate)

DSC

AA9-CBM1

ND

Kittl et al. [30]

NcLPMO9J

66.9

6.0 (phosphate)

DSC

AA9-CBM1

ND

Kittl et al. [30]

NcLPMO9F

68.9

6.0 (phosphate)

DSC

AA9

ND

Kittl et al. [30]

NcLPMO9E

67.9

6.0 (phosphate)

DSC

AA9-CBM1

ND

Kittl et al. [30]

PvLPMO9A-holo

59.6

7.0 (Polybuffer 96, GE Healthcare)

DSC

AA9-C-termd

ND

Semenova et al. [50]

PvLPMO9A-apo

49.9

7.0 (Polybuffer 96, GE Healthcare)

DSC

AA9-C-termd

ND

Semenova et al. [50]

  1. Ligands or other molecules present during the determination of the apparent melting temperature are provided with the enzyme names
  2. ND not detected, DSC differential scanning calorimetry, DSF differential scanning fluorimetry, ITF intrinsic Trp fluorescence, CD circular dichroism
  3. aThe term “holo” refers to the enzyme with copper bound, while “apo” refers to the metal free enzyme; the presence of other metals and/or substrates is indicated. If nothing is written by the enzyme name, the experiment was performed with unknown copper content
  4. bTemperatures estimated based on CD diagrams in Frommhagen et al. [49]
  5. cThe table only shows a selection of stability data presented in the study by Kracher et al. [44]
  6. dC-terminal peptide of unknown function