Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes

Nuno Borges, Ana Ramos, Neil D.H. Raven, Richard J. Sharp, Helena Santos

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

The protection of mannosylglycerate, at 0.5 M concentration, against heat inactivation of the model enzyme lactate dehydrogenase (LDH) was compared to that exerted by other compatible solutes, namely, trehalose, ectoine, hydroxyectoine, di-myo-inositol phosphate, diglycerol phosphate, and mannosylglyceramide. Mannosylglycerate and hydroxyectoine were the best stabilizers of the enzyme and showed comparable protective effects. Diglycerol phosphate, trehalose, and mannosylglyceramide protected the enzyme to a lower extent. Ectoine conferred no protection, and di-myo-inositol phosphate had a strong destabilizing effect. The superior ability of mannosylglycerate to prevent LDH inactivation was accompanied by a higher efficiency in preventing LDH aggregation induced by heat stress. Moreover, mannosylglycerate induced an increase of 4.5°C in the melting temperature of LDH, whereas the same molar concentration of trehalose caused an increase of only 2.2°C. The effectiveness of mannosylglycerate in protecting LDH was also compared to that of other chemically related compounds: mannose, methyl-mannoside, potassium glycerate, glucosylglycerol, glycerol, and glucose. Mannosylglycerate conferred the highest protection, but glucosylglycerol and potassium glycerate were very efficient; glucose exerted a low degree of protection, glycerol and methyl-mannoside had no significant effect, and mannose caused destabilization. Mannosylglycerate was also a good thermoprotectant of glucose oxidase from Aspergillus niger, an enzyme with a net charge opposite to that of LDH under the working conditions. Given the superior performance of mannosylglycerate as a thermoprotectant of enzyme activity in vitro, it is conceivable that it also fulfills a protein thermoprotective function in vivo.

Original languageEnglish
Pages (from-to)209-216
Number of pages8
JournalExtremophiles
Volume6
Issue number3
DOIs
Publication statusPublished - 1 Dec 2002

Fingerprint

L-Lactate Dehydrogenase
Enzymes
Trehalose
Inositol Phosphates
Mannose
Glycerol
Potassium
Hot Temperature
Glucose
Glucose Oxidase
Aspergillus niger
mannosylglycerate
Freezing
Temperature
Proteins

Keywords

  • Compatible solutes
  • Lactate dehydrogenase
  • Mannosylglycerate
  • Thermal stabilization

Cite this

@article{675c88da06084088bbd8f4259b064bdf,
title = "Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes",
abstract = "The protection of mannosylglycerate, at 0.5 M concentration, against heat inactivation of the model enzyme lactate dehydrogenase (LDH) was compared to that exerted by other compatible solutes, namely, trehalose, ectoine, hydroxyectoine, di-myo-inositol phosphate, diglycerol phosphate, and mannosylglyceramide. Mannosylglycerate and hydroxyectoine were the best stabilizers of the enzyme and showed comparable protective effects. Diglycerol phosphate, trehalose, and mannosylglyceramide protected the enzyme to a lower extent. Ectoine conferred no protection, and di-myo-inositol phosphate had a strong destabilizing effect. The superior ability of mannosylglycerate to prevent LDH inactivation was accompanied by a higher efficiency in preventing LDH aggregation induced by heat stress. Moreover, mannosylglycerate induced an increase of 4.5°C in the melting temperature of LDH, whereas the same molar concentration of trehalose caused an increase of only 2.2°C. The effectiveness of mannosylglycerate in protecting LDH was also compared to that of other chemically related compounds: mannose, methyl-mannoside, potassium glycerate, glucosylglycerol, glycerol, and glucose. Mannosylglycerate conferred the highest protection, but glucosylglycerol and potassium glycerate were very efficient; glucose exerted a low degree of protection, glycerol and methyl-mannoside had no significant effect, and mannose caused destabilization. Mannosylglycerate was also a good thermoprotectant of glucose oxidase from Aspergillus niger, an enzyme with a net charge opposite to that of LDH under the working conditions. Given the superior performance of mannosylglycerate as a thermoprotectant of enzyme activity in vitro, it is conceivable that it also fulfills a protein thermoprotective function in vivo.",
keywords = "Compatible solutes, Lactate dehydrogenase, Mannosylglycerate, Thermal stabilization",
author = "Nuno Borges and Ana Ramos and Raven, {Neil D.H.} and Sharp, {Richard J.} and Helena Santos",
year = "2002",
month = "12",
day = "1",
doi = "10.1007/s007920100236",
language = "English",
volume = "6",
pages = "209--216",
journal = "Extremophiles",
issn = "1431-0651",
publisher = "Springer",
number = "3",

}

Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. / Borges, Nuno; Ramos, Ana; Raven, Neil D.H.; Sharp, Richard J.; Santos, Helena.

In: Extremophiles, Vol. 6, No. 3, 01.12.2002, p. 209-216.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes

AU - Borges, Nuno

AU - Ramos, Ana

AU - Raven, Neil D.H.

AU - Sharp, Richard J.

AU - Santos, Helena

PY - 2002/12/1

Y1 - 2002/12/1

N2 - The protection of mannosylglycerate, at 0.5 M concentration, against heat inactivation of the model enzyme lactate dehydrogenase (LDH) was compared to that exerted by other compatible solutes, namely, trehalose, ectoine, hydroxyectoine, di-myo-inositol phosphate, diglycerol phosphate, and mannosylglyceramide. Mannosylglycerate and hydroxyectoine were the best stabilizers of the enzyme and showed comparable protective effects. Diglycerol phosphate, trehalose, and mannosylglyceramide protected the enzyme to a lower extent. Ectoine conferred no protection, and di-myo-inositol phosphate had a strong destabilizing effect. The superior ability of mannosylglycerate to prevent LDH inactivation was accompanied by a higher efficiency in preventing LDH aggregation induced by heat stress. Moreover, mannosylglycerate induced an increase of 4.5°C in the melting temperature of LDH, whereas the same molar concentration of trehalose caused an increase of only 2.2°C. The effectiveness of mannosylglycerate in protecting LDH was also compared to that of other chemically related compounds: mannose, methyl-mannoside, potassium glycerate, glucosylglycerol, glycerol, and glucose. Mannosylglycerate conferred the highest protection, but glucosylglycerol and potassium glycerate were very efficient; glucose exerted a low degree of protection, glycerol and methyl-mannoside had no significant effect, and mannose caused destabilization. Mannosylglycerate was also a good thermoprotectant of glucose oxidase from Aspergillus niger, an enzyme with a net charge opposite to that of LDH under the working conditions. Given the superior performance of mannosylglycerate as a thermoprotectant of enzyme activity in vitro, it is conceivable that it also fulfills a protein thermoprotective function in vivo.

AB - The protection of mannosylglycerate, at 0.5 M concentration, against heat inactivation of the model enzyme lactate dehydrogenase (LDH) was compared to that exerted by other compatible solutes, namely, trehalose, ectoine, hydroxyectoine, di-myo-inositol phosphate, diglycerol phosphate, and mannosylglyceramide. Mannosylglycerate and hydroxyectoine were the best stabilizers of the enzyme and showed comparable protective effects. Diglycerol phosphate, trehalose, and mannosylglyceramide protected the enzyme to a lower extent. Ectoine conferred no protection, and di-myo-inositol phosphate had a strong destabilizing effect. The superior ability of mannosylglycerate to prevent LDH inactivation was accompanied by a higher efficiency in preventing LDH aggregation induced by heat stress. Moreover, mannosylglycerate induced an increase of 4.5°C in the melting temperature of LDH, whereas the same molar concentration of trehalose caused an increase of only 2.2°C. The effectiveness of mannosylglycerate in protecting LDH was also compared to that of other chemically related compounds: mannose, methyl-mannoside, potassium glycerate, glucosylglycerol, glycerol, and glucose. Mannosylglycerate conferred the highest protection, but glucosylglycerol and potassium glycerate were very efficient; glucose exerted a low degree of protection, glycerol and methyl-mannoside had no significant effect, and mannose caused destabilization. Mannosylglycerate was also a good thermoprotectant of glucose oxidase from Aspergillus niger, an enzyme with a net charge opposite to that of LDH under the working conditions. Given the superior performance of mannosylglycerate as a thermoprotectant of enzyme activity in vitro, it is conceivable that it also fulfills a protein thermoprotective function in vivo.

KW - Compatible solutes

KW - Lactate dehydrogenase

KW - Mannosylglycerate

KW - Thermal stabilization

UR - http://www.scopus.com/inward/record.url?scp=0036599177&partnerID=8YFLogxK

U2 - 10.1007/s007920100236

DO - 10.1007/s007920100236

M3 - Article

VL - 6

SP - 209

EP - 216

JO - Extremophiles

JF - Extremophiles

SN - 1431-0651

IS - 3

ER -