1998
DOI: 10.1590/s1516-89131998000200002
|View full text |Cite
|
Sign up to set email alerts
|

Peroxidase from peach fruit: thermal Stability

Abstract: Peroxidase from peach fruit was purified 28.9-fold by

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
19
0

Year Published

2002
2002
2015
2015

Publication Types

Select...
6

Relationship

1
5

Authors

Journals

citations
Cited by 19 publications
(20 citation statements)
references
References 32 publications
(27 reference statements)
1
19
0
Order By: Relevance
“…The optimum temperature was 40°C and 40% of the maximum activity was registered at 55°C indicating a heat labile enzyme. The apparent activation energy (Ea) value for product formation was found to be 10.04 kcal/mol, in contrast the temperature coeficient (Q 10 ) calculated from this Ea value was 1.78 in the range of 20-30°C, a similar value found for other peroxidases (Bruemmer et al, 1976, Joffe & Ball, 1962, Neves & Lourenço, 1998, Lourenço et al, 1995. Figure 4 shows the time course inactivation of purified peach ionically bound POD from 60 to 75°C.…”
Section: Properties Of Sephadex G-100 Purified Enzymementioning
confidence: 57%
See 3 more Smart Citations
“…The optimum temperature was 40°C and 40% of the maximum activity was registered at 55°C indicating a heat labile enzyme. The apparent activation energy (Ea) value for product formation was found to be 10.04 kcal/mol, in contrast the temperature coeficient (Q 10 ) calculated from this Ea value was 1.78 in the range of 20-30°C, a similar value found for other peroxidases (Bruemmer et al, 1976, Joffe & Ball, 1962, Neves & Lourenço, 1998, Lourenço et al, 1995. Figure 4 shows the time course inactivation of purified peach ionically bound POD from 60 to 75°C.…”
Section: Properties Of Sephadex G-100 Purified Enzymementioning
confidence: 57%
“…Enzyme assay: Soluble and ionically bound peroxidase activities were determined by change in absorbance at 460 nm due to o -dianisidine oxidation in the presence of hydrogen peroxide and the enzyme (Neves & Lourenço, 1998). The reaction mixture consisted of 0.2 ml 15 mM Odianisidine; 0.2 ml 10 mM hydrogen peroxide, 0.1 M potassium phosphate-citrate buffer, pH 5.0 in a total volume of 3.0 ml.…”
Section: Methodsmentioning
confidence: 99%
See 2 more Smart Citations
“…Similarly highest activities were shown in case of tobacco leaf at 70°C, (Silva et al, 1990), in Ricinus at 60°C (Ryan et al 1994), in lima bean (Phaseolus limensis) seed at 55°C (Wang et al 2008), in sunflower at 50°C (Hager et al 2008) and in peach fruit at 40°C (Neves 2002;Neves and Lourenço 1998) and a ranges of 40-70°C…”
Section: Effect Of Temperaturementioning
confidence: 76%