Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution

Typeset version

 

TY  - JOUR
  - Lemos, MA,Oliveira, JC,Saraiva, JA
  - 2000
  - Unknown
  - LWT - Food Science and Technology
  - Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution
  - Validated
  - ()
  - enzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY
  - 33
  - 362
  - 368
  - The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press.
DA  - 2000/NaN
ER  - 
@article{V43338894,
   = {Lemos,  MA and Oliveira,  JC and Saraiva,  JA },
   = {2000},
   = {Unknown},
   = {LWT - Food Science and Technology},
   = {Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution},
   = {Validated},
   = {()},
   = {enzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY},
   = {33},
  pages = {362--368},
   = {{The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press.}},
  source = {IRIS}
}
AUTHORSLemos, MA,Oliveira, JC,Saraiva, JA
YEAR2000
MONTHUnknown
JOURNAL_CODELWT - Food Science and Technology
TITLEInfluence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDenzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY
VOLUME33
ISSUE
START_PAGE362
END_PAGE368
ABSTRACTThe thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press.
PUBLISHER_LOCATION
ISBN_ISSN
EDITION
URL
DOI_LINK
FUNDING_BODY
GRANT_DETAILS