Thermal Stability of Dehydrated α-Amylase in Trehalose Matrices in Relation to its Phase Transitions
Thermal stability of α-amylase in trehalose matrices of reduced moisture content was studied as affected by phase transitions occurring as a result of increasing temperature at a moisture content of 50 g/kg. Removal of water greatly enhanced thermal stability of α-amylase but when trehalose was pres...
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1997
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| LEADER | 09953caa a22008057a 4500 | ||
|---|---|---|---|
| 001 | PAPER-3217 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203241.0 | ||
| 008 | 190411s1997 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0000521006 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Terebiznik, M.R. | |
| 245 | 1 | 0 | |a Thermal Stability of Dehydrated α-Amylase in Trehalose Matrices in Relation to its Phase Transitions |
| 260 | |c 1997 | ||
| 270 | 1 | 0 | |m Terebiznik, M.R.; Depto. de Ing. Química, Universidad de Buenos Aires, (1428), Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Tan, C.S., Van Ingen, C.W., Talsma, H., Van Mileternburg, J.C., Steffensen, C.L., Vlug, I.J.A., Stalpers, J.A., Freeze-drying of fungi: Influence of composition and glass transition temperature of the protectant (1995) Cryobiology, 32, pp. 60-67 | ||
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| 520 | 3 | |a Thermal stability of α-amylase in trehalose matrices of reduced moisture content was studied as affected by phase transitions occurring as a result of increasing temperature at a moisture content of 50 g/kg. Removal of water greatly enhanced thermal stability of α-amylase but when trehalose was present an extraordinary stabilization was achieved. Even in an initially rubbery condition, the protective effect of trehalose could be assessed up to 100 °C. Deactivation kinetics in the range 80-100 °C were related to crystallization of amorphous trehalose which would occur because the system was above the glass transition temperature. According to available water, at most 50% of amorphous trehalose would crystallize. The remaining amorphous trehalose phase would increase its glass transition temperature leading to enhanced enzyme stability. At temperatures close to 90 °C, trehalose dihydrate crystals start melting, releasing water which could promote further trehalose crystallization and enzyme deactivation. Once trehalose crystallizes, the protective effect may be lost since crystalline trehalose forms a separated phase no longer associated with the enzyme. These phase transitions were reflected as breaks in the Arrhenius plots. © 1997 Academic Press Limited. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Secretaría de Ciencia y Técnica, Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: The authors acknowledge financial support from the University of Buenos Aires (Secretaría de Ciencia y Técnica), Consejo Nacional de Investigaciones Cientifi-cas y Técnicas de la República Argentina, and International Foundation for Science (Sweden). We thank Dr Marcus Karel for his helpful comments and Dr Jorge Wagner for his technical assistance in DSC measurements. | ||
| 593 | |a Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, (1428), Buenos Aires, Argentina | ||
| 593 | |a Depto. de Ing. Química, Universidad de Buenos Aires, (1428), Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a Α-AMYLASE |
| 690 | 1 | 0 | |a PHASE TRANSITIONS |
| 690 | 1 | 0 | |a STABILITY |
| 690 | 1 | 0 | |a TREHALOSE |
| 690 | 1 | 0 | |a ARRHENIUS |
| 700 | 1 | |a Buera, M.P. | |
| 700 | 1 | |a Pilosof, A.M.R. | |
| 773 | 0 | |d 1997 |g v. 30 |h pp. 513-518 |k n. 5 |p LWT - Food Sci. Technol. |x 00236438 |w (AR-BaUEN)CENRE-292 |t LWT - Food Science and Technology | |
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