The heat stability and isoenzyme composition of peroxidases in Ohane grapes

D. S. Robinson; M. Bretherick; Judith Donnelly

doi:10.1111/j.1365-2621.1989.tb00687.x

The heat stability and isoenzyme composition of peroxidases in Ohane grapes

D. S. Robinson, M. Bretherick , Judith Donnelly

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

Soluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non-linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.

Original language	English
Pages (from-to)	613-18
Number of pages	6
Journal	International Journal of Food Science and Technology
Volume	24
Issue number	6
DOIs	https://doi.org/10.1111/j.1365-2621.1989.tb00687.x
Publication status	Published - Dec 1989

Keywords

Grape peroxidases
Isoenzymes
Regeneration
Thin layer isoelectric focusing

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10.1111/j.1365-2621.1989.tb00687.x

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title = "The heat stability and isoenzyme composition of peroxidases in Ohane grapes",

abstract = "Soluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non-linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.",

keywords = "Grape peroxidases, Isoenzymes, Regeneration, Thin layer isoelectric focusing",

author = "Robinson, {D. S.} and M. Bretherick and Judith Donnelly",

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TY - JOUR

T1 - The heat stability and isoenzyme composition of peroxidases in Ohane grapes

AU - Robinson, D. S.

AU - Bretherick , M.

AU - Donnelly, Judith

PY - 1989/12

Y1 - 1989/12

N2 - Soluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non-linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.

AB - Soluble and ionically bound peroxidases have been obtained from homogenized Ohane grapes. The soluble fraction contained the highest level of peroxidase activity and accounted for approximately 87% of the total enzymic activity. Plots of the percentage of heat inactivation for the grape peroxidases against time were non-linear with approximately 90% of the peroxidase activity being destroyed after 10 min at 80°C. Following heat inactivation there was no significant regeneration of enzymic activity. Using isoelectric focusing six isoperoxidases with isoelectric points ranging from approximately pI 3.5 to 9.8 were detected.

KW - Grape peroxidases

KW - Isoenzymes

KW - Regeneration

KW - Thin layer isoelectric focusing

U2 - 10.1111/j.1365-2621.1989.tb00687.x

DO - 10.1111/j.1365-2621.1989.tb00687.x

M3 - Article

SN - 1365-2621

VL - 24

SP - 613

EP - 618

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

IS - 6

ER -

The heat stability and isoenzyme composition of peroxidases in Ohane grapes

Abstract

Keywords

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