Role of sucrose-LDH hydrogen bond for thermal stabilizing effect of sucrose on freeze-dried LDH

T. Suzuki, K. Imamura, H. Fujimoto, M. Okazaki

Research output: Contribution to journalConference article

6 Citations (Scopus)

Abstract

Relationship between thermal stabilizing effect of sugar on freeze-dried protein and sugar-protein hydrogen bond is studied. Sucrose and lactate dehydrogenase (LDH) are used as models for sugar and protein. Samples of freeze-dried LDH involved in sucrose of different crystallinity were prepared, and measurement of X-ray diffractometry (XRD) and Fourier-Transform Infrared (FT-IR) spectroscopy was done. It is found that when sucrose is amorphous, the degree of hydrogen bond formation is high and LDH is stabilized: when sucrose is crystalline, hydrogen bond is less formed and LDH is inactivated. These results indicate that the stabilizing effect of sugar is closely related to sugar-protein hydrogen bond. It is also found that there is an optimum sucrose content for the thermal stabilizing effect. This is because amorphous structure of sucrose is stabilized and protected from crystallization by LDH. Thus we can deduce that sugars and proteins work together to keep the activities of proteins.

Original languageEnglish
Pages (from-to)1429-1439
Number of pages11
JournalDrying Technology
Volume17
Issue number7-8
DOIs
Publication statusPublished - Jan 1 1999
Externally publishedYes
EventProceedings of the 1998 11th International Drying Sympoisum IDS'98 - Halkidiki, Greece
Duration: Aug 19 1998Aug 22 1998

Keywords

  • Freeze drying
  • Hydrogen bond
  • Lactate dehydrogenase
  • Sucrose
  • Thermal stabilization

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Physical and Theoretical Chemistry

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