ฉันรักการแปลHeat treatments, varyin

ฉันรักการแปล
Heat treatments, varying levels of protein, ionic strength and pH, in addition to
the molecular interactions among food processing, which affect certain physicochemical
properties in resulting gels of commercial soy isolates ( > 90% protein)
are discussed. Calorimetric measurements were used to describe a partially
denatured molecular order and conclude that temperature and the heating rate of
temperature are expected to correlate strongly to the macromolecular conformational
changes. Structural characterisation with small deformation rheological
measurements (elastic modulus, tan S, creep/compliance) was performed for a
series of soy protein with the temperature treatments ranging from 30 to 90°C in
an attempt to examine the mechanisms involved. Aggregate gels were observed at
lower temperatures (up to 60°C preheat treatment) with maximum network
rigidity, which is associated with the different degrees of ‘pregelation’ stages
during the production process. ‘Disaggregation’ at higher temperatures treatments
weakened the molecular association and produced more elastic, finestranded
gels. Essentially, disulphide linkages on heated networks and mainly
non-covalent physical forces of attraction in their cooled counterparts, contributed
to the nature of gels’ behaviour, while the involvement of hydrophobic
interaction was negligible. Lower concentrations were more sensitive to temperature
factor. Similar conclusions on the structure and rigidity were also
observed from long-time creep experiments. Both covalent and non-covalent
topological interactions, which are involved in the heated (90°C) network stabilisation,
contributed proportionally with concentration to the viscoelastic constants
from a six-element mechanical model. Heated protein aqueous
preparations with urea, a structure perturbing agent, produced entropically elastic
networks, with substantial homogeneity, but still significant enthalpic contribution
was observed. Textural changes due to sensitivity on ionic strength and
pH were investigated for different soy protein concentrations, using texture analysis
compression measurements. The presence of salt strengthened the interaggregate
forces, promoted aggregation and, therefore, stabilised the structure of
partially denatured soy protein gels. Copyright 6 1996 Published by Elsevier

ผลลัพธ์ (อังกฤษ) 1:

I love the translation.Heat treatments, varying levels of protein, ionic strength and pH, in addition tothe molecular interactions among food processing, which affect certain physicochemicalproperties in resulting gels of commercial soy isolates ( > 90% protein)are discussed. Calorimetric measurements were used to describe a partiallydenatured molecular order and conclude that temperature and the heating rate oftemperature are expected to correlate strongly to the macromolecular conformationalchanges. Structural characterisation with small deformation rheologicalmeasurements (elastic modulus, tan S, creep/compliance) was performed for aseries of soy protein with the temperature treatments ranging from 30 to 90°C inan attempt to examine the mechanisms involved. Aggregate gels were observed atlower temperatures (up to 60°C preheat treatment) with maximum networkrigidity, which is associated with the different degrees of 'pregelation' stagesduring the production process. 'Disaggregation' at higher temperatures treatmentsweakened the molecular association and produced more elastic, finestrandedgels. Essentially, disulphide linkages on heated networks and mainlynon-covalent physical forces of attraction in their cooled counterparts, contributedto the nature of gels' behaviour, while the involvement of hydrophobicinteraction was negligible. Lower concentrations were more sensitive to temperaturefactor. Similar conclusions on the structure and rigidity were alsoobserved from long-time creep experiments. Both covalent and non-covalenttopological interactions, which are involved in the heated (90°C) network stabilisation,contributed proportionally with concentration to the viscoelastic constantsfrom a six-element mechanical model. Heated protein aqueouspreparations with urea, a structure perturbing agent, produced entropically elasticnetworks, with substantial homogeneity, but still significant enthalpic contributionwas observed. Textural changes due to sensitivity on ionic strength andpH were investigated for different soy protein concentrations, using texture analysiscompression measurements. The presence of salt strengthened the interaggregateforces, promoted aggregation and, therefore, stabilised the structure ofpartially denatured soy protein gels. Copyright 6 1996 Published by Elsevier

ผลลัพธ์ (อังกฤษ) 2:

I love to translate
Heat Treatments, varying levels of protein, Ionic strength and pH, in addition to
The molecular Interactions Among Food processing, which affect Certain physicochemical
Properties in resulting gels of Commercial soy isolates (> 90% protein)
are discussed. calorimetric measurements. were Used to describe a partially
Denatured molecular Order and conclude that Temperature and The heating rate of
Temperature are expected to correlate Strongly to The macromolecular conformational
Changes. Structural characterization with Small deformation rheological
measurements (Elastic modulus, Tan S, Creep / Compliance) was performed. for a
Series of soy protein with The Temperature Treatments ranging from 30 to 90 ° C in
an attempt to examine The Mechanisms Involved. Aggregate gels were observed at
Lower temperatures (up to 60 ° C Preheat Treatment) with Maximum Network
rigidity, which is Associated. with The different Degrees of 'Pregelation' Stages
during The production Process. 'disaggregation' at Higher temperatures Treatments
weakened The molecular association and produced more Elastic, Finestranded
gels. Essentially, disulphide Linkages on heated Networks and mainly
non-Covalent physical Forces of attraction in. their cooled counterparts, Contributed
to The Nature of gels' behavior, while The involvement of hydrophobic
Interaction was negligible. Lower concentrations were more sensitive to Temperature
factor. Similar conclusions on The structure and rigidity were also
observed from long-time Creep experiments. Both Covalent. and non-Covalent
topological Interactions, which are Involved in The heated (90 ° C) Network stabilization,
Contributed Proportionally with Concentration to The viscoelastic constants
from a Six-Element mechanical Model. Heated protein AQUEOUS
preparations with urea, a structure Perturbing Agent, produced. entropically Elastic
Networks, with substantial homogeneity, but Still significant Enthalpic contribution
was observed. Textural Changes Due to sensitivity on Ionic strength and
pH were Investigated for different soy protein concentrations, using texture analysis
compression measurements. The Presence of Salt strengthened The Interaggregate
Forces, promoted. aggregation and, Therefore, stabilized The structure of
partially Denatured soy protein gels. Copyright 6 1996th Published by Elsevier.