The thermal inactivation kinetics of freeze-dried á-amylase in a solid matrix was studied at water contents ranging from 1.5 to 23.9 g water per 100 g dry solid. These conditions were obtained by equilibration in dry environments, with water activities ranging between 0.11 and 0.88. Isothermal inactivation experiments in the range 135 to 150 °C were performed. Results were analysed with both the Bigelow and Arrhenius models. It was concluded that there was no statistical significance to suggest that the water content influenced the kinetic parameters. An activation energy of 128 kJ/mol and pre-exponential factor with a logarithm of 33.9 described all the results well
THOMPSON, P. J. (University of Nebraska, Lincoln) AND T. L. THOMPSON. Some characteristics of a puri...
A comprehensive experimental study of the drying of enzymes (E) and gin seng (GS) biomaterials provi...
Enzymes typically have a critical instability, which dominates both formulation and process developm...
The thermal inactivation of suspensions of á-amylase from Bacillus amyloliquefaciens equilibrated at...
The activity and thermal stability of α-amylase were studied in the presence of different conce...
The primary target of this work was the development of enzyme based time-temperature integrators (TT...
Enzymes are often dried for stability reasons and to facilitate handling. However, they are often su...
This study is aimed at comparing two traditional methods of drying of enzymes and at verifying the e...
AbstractStudies on the irreversible thermoinactivation of β-amylase from Bacillus megaterium B6 expo...
Ab s t r a c t. The thermal degradation of Aspergillus oryzae α-amylase in the presence of sug-ars (...
This study investigated the ability of Bacillus cereus MTCC-1305 to produce alpha amylase and its ki...
The kinetics of non-enzymatic browning (NEB) was studied in freeze-dried model and food systems in a...
Abstract Bovine serum albumin (BSA) as a modifier was used with glutaraldehyde as a binder to study ...
437-442Highest α-amylase activity of Brevibacillus borstelensis R1 was observed at 370C (6133±58U/ml...
AbstractHyperthermophilic enzymes are of industrial importance and interest, especially due to their...
THOMPSON, P. J. (University of Nebraska, Lincoln) AND T. L. THOMPSON. Some characteristics of a puri...
A comprehensive experimental study of the drying of enzymes (E) and gin seng (GS) biomaterials provi...
Enzymes typically have a critical instability, which dominates both formulation and process developm...
The thermal inactivation of suspensions of á-amylase from Bacillus amyloliquefaciens equilibrated at...
The activity and thermal stability of α-amylase were studied in the presence of different conce...
The primary target of this work was the development of enzyme based time-temperature integrators (TT...
Enzymes are often dried for stability reasons and to facilitate handling. However, they are often su...
This study is aimed at comparing two traditional methods of drying of enzymes and at verifying the e...
AbstractStudies on the irreversible thermoinactivation of β-amylase from Bacillus megaterium B6 expo...
Ab s t r a c t. The thermal degradation of Aspergillus oryzae α-amylase in the presence of sug-ars (...
This study investigated the ability of Bacillus cereus MTCC-1305 to produce alpha amylase and its ki...
The kinetics of non-enzymatic browning (NEB) was studied in freeze-dried model and food systems in a...
Abstract Bovine serum albumin (BSA) as a modifier was used with glutaraldehyde as a binder to study ...
437-442Highest α-amylase activity of Brevibacillus borstelensis R1 was observed at 370C (6133±58U/ml...
AbstractHyperthermophilic enzymes are of industrial importance and interest, especially due to their...
THOMPSON, P. J. (University of Nebraska, Lincoln) AND T. L. THOMPSON. Some characteristics of a puri...
A comprehensive experimental study of the drying of enzymes (E) and gin seng (GS) biomaterials provi...
Enzymes typically have a critical instability, which dominates both formulation and process developm...