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 language | English |
|---|---|
| Pages (from-to) | 1429-1439 |
| Number of pages | 11 |
| Journal | Drying Technology |
| Volume | 17 |
| Issue number | 7-8 |
| Publication status | Published - 1999 |
| Externally published | Yes |
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Keywords
- Freeze drying
- Hydrogen bond
- Lactate dehydrogenase
- Sucrose
- Thermal stabilization
ASJC Scopus subject areas
- Chemical Engineering (miscellaneous)
Cite this
Role of sucrose-LDH hydrogen bond for thermal stabilizing effect of sucrose on freeze-dried LDH. / Suzuki, T.; Imamura, Koreyoshi; Fujimoto, H.; Okazaki, M.
In: Drying Technology, Vol. 17, No. 7-8, 1999, p. 1429-1439.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Role of sucrose-LDH hydrogen bond for thermal stabilizing effect of sucrose on freeze-dried LDH
AU - Suzuki, T.
AU - Imamura, Koreyoshi
AU - Fujimoto, H.
AU - Okazaki, M.
PY - 1999
Y1 - 1999
N2 - 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.
AB - 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.
KW - Freeze drying
KW - Hydrogen bond
KW - Lactate dehydrogenase
KW - Sucrose
KW - Thermal stabilization
UR - http://www.scopus.com/inward/record.url?scp=0033489896&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033489896&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0033489896
VL - 17
SP - 1429
EP - 1439
JO - Drying Technology
JF - Drying Technology
SN - 0737-3937
IS - 7-8
ER -