135 
 

Journal homepage: www.fia.usv.ro/fiajournal 
Journal of Faculty of Food Engineering,  

Ştefan cel Mare University of Suceava, Romania  
Volume XII, Issue 2 – 2013, pag. 135 - 142 

 
 
 

CHANGES OF SOME DEHYDROGENASE ACTIVITIES IN THE 

LEAVES OF PEACH CULTIVAR SPRINGCREST NATURALLY 

INFECTED WITH THE FUNGUS TAPHRINA DEFORMANS 
 

*Rodica CIOBANU1 
 

1Alexandru Ioan Cuza University,Faculty of Biology, Iaşi, Romania 
ciobanu.rodica1981@yahoo.com 
*Corresponding author 

Received June 9th 2013, accepted June28th 2013 
 
 

Abstract: The influence of Taphrina deformans (Berk.) Tul., associated with peach leaf curl 
disease,on glucose dehydrogenase (EC 1.1.99.10), isocitrate dehydrogenase (EC 1.1.1.42), α-
ketoglutarate dehydrogenase (EC 1.2.4.2) and malate dehydrogenase (EC 1.1.1.37) activitities in the 
leaves harvested from peachcultivar Springcrest, was investigated. Samples of both healthy and 
diseased leaves were analyzed. The resultus of this study suggests that the leaves infection with the 
biotrophic fungus Taphrina deformans lead to the decreasing of glucose dehydrogenase and malate 
dehydrogenase activities and to a significantlly increasing of isocitrate dehydrogenase and α-
ketoglutarate dehydrogenase activities as an attempt of host plant tissues to limit the damages caused 
by the fungus attack. Data obtained in this study revealed significant differences in these enzymes 
activities depending on the type of theenzyme, the age of the leaves and the presence or absence of 
fungus attack. 

 
Keywords:peach leaf curl, glucose dehydrogenase, isocitrate dehydrogenase, α-ketoglutarate 
dehydrogenase, malate dehydrogenase 
 

1. Introduction 

Persica vulgaris Mill. is one of the major 
fruit crop in Romania, in present it is 
occuping the third place after apples and 
plums [1]. 
Peach leaf curl disease caused by Taphrina 
deformans (Berk.) Tul.is predominant in all 
the peach growing areas of the world [2] 
and is one of the most dangerous disease 
for peach because it can cause the 
defoliation and major crop loss at nearly 
all cultivars of peach trees.The infection is 
favoured by low temperature and high 
humidity from the time of bud swellen; the 
infection occurs mainly during a short 
period after the buds open when the new 
tissues are susceptible and as all organs 

grow older they become resistant to 
infection [3].  
Dehydrogenases are oxidizing enzymes 
which catalyze the electron transfer from 
the donor to an acceptor other than 
molecular oxigen.  
Glucose dehydrogenase (GHD, D-glucose: 
acceptor 1-oxidoreductase, EC 1.1.99.10) 
is a FAD-dependent enzyme. Glucose 
dehydrogenase is anoxidoreductase that 
catalyze the first hydroxyl group of glucose 
and other sugar molecules, utilizing FAD 
as primaryelectronacceptor. FAD GDHs 
utilize a variety of external electron 
acceptors, but not oxygen; glucose 
dehydrogenase has been found as 
extracellular enzyme in fungi, such as 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

136 
 

Aspergillus sp., and it has ahigh 
specificityfor glucose [4]. Intracellular 
FAD-dependent GDH is involved 
inmetabolic pathways, such as the glycan 
metabolism and the biosynthesis of 
secondary metabolites; they are suggested 
to play a role in the pentose phosphate 
pathway involving glucose turnover for the 
production of NADH as reducing 
equivalents and pentoses as integral parts 
of nucleotides. The biological function of 
extracellular FAD-dependent glucose 
dehydrogenase is still unclear, but a role 
during fungal attack on the host-plant is 
proposed. By reducing quinones and 
phenoxy radicals glucose dehydrogenase is 
able to neutralize the action of plant 
laccases, phenoloxidases or peroxidases, 
which are used by infected plant tissues to 
limit the fungal attack [5]. 
Isocitrate dehydrogenase (IDH, EC 
1.1.1.42) is a NADP-dependent enzyme, 
that controls the carbon flux between the 
Krebs cycle and the glyoxylate bypass via 
its activation and inactivation by the 
bifunctional IDH kinase/phosphatase. 
Thus, the activation of isocitrate 
dehydrogenase forces the flow through the 
Krebs cycle, causing a decrease in the 
intracellular isocitrate level and an increase 
in the α-ketoglutarate level [6]. 
α-ketoglutarate dehydrogenase (α-KGDH, 
EC 1.2.4.2), a key regulatory point of 
tricarboxylic acid cycle, plays vital roles in 
the multiple pathways of energy 
metabolism and biosynthesis [7]. α-
ketoglutarate dehydrogenase is an enzyme 
which catalyses the non-equilibrium 
reaction converting α-ketoglutarate, 
coenzyme A and NAD+ to succinyl-CoA, 
NADH and CO2, requiring thiamine 
pyrophosphate as a cofactor [8]. It 
transfers four-carbon aldehyde group from 
α-ketoglutarate to thiamine 
phyrophosphate to form hydroxyethyl-
thiamine phyrophosphate. 

Malate dehydrogenase (MDH, L-malate: 
NAD+ oxidoreductase, EC 1.1.1.37) 
catalyzes the conversion of oxaloacetate 
and malate utilizing the NAD or NADP 
coenzyme system. Malate dehydrogenase 
is found in cytosol where it participates in 
malate/aspartate shuttle and in the 
mitochondrial matrix where it has a key 
role in the citric acid cycle and are NAD-
dependent enzymes; the malate 
dehydrogenase found in plant chloroplasts 
has NADP as coenzyme [9]. 
 
2. Materials and methods 
 
Vegetal material used in this study was 
represented by fresh healthy leaves and 
leaves naturally infected with the fungus 
Taphrina deformans, harvested, starting to 
middle of April until late June in year 2008, 
from peach cv. Springcrest, from the 
experimental orchard “Vasile Adamachi” 
Iaşi. The determinations of the 
dehydrogenases activity were made at: 19 
April (I), 7 (II), 19 (III) and 27 (IV) May, 3 
(V), 10 (VI) and 22 (VII) June. 
Springcrest cv. is considered to be very 
susceptilbe to this pathogen attack [10,11]. 
The leaves were harvested early in the 
morning and enzymes activity was 
estimated in the same day. 
The dehydrogenases activity was 
determinated by Sîsoev and Krasna 
spectrophotometric method, modified by 
Artenie.  
This method has at basis the ability of 
dehydrogenases to transfer hydrogen from 
various substrate (glucose, isocitric acid, α-
ketoglutaric acid and malic acid) to 2,3,5-
triphenil-tetrazolium-chloride (TTC) which 
is reduced to triphenyl formazan colored in 
red. 
Samples collected were first washed with 
distilled water, then the enzymes were 
extracted using 3 ml of phosphate buffer 
pH-7,4. The assay mixture of 
dehydrogenases contained: 0,25 ml of 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

137 
 

crude enzyme extract, 0,2 ml of specific 
substrate 0,2 M, pH-7,4, 0,75 ml distillated 
water and 0,2 ml of standard solution of 
2,3,5-triphenil-tetrazolium-chloride 1%. In 
the control tests the specific substrate was 
replaced with the same quantity of 
phosphate buffer.  
The tests were incubated 18 hours in a 
thermostat at 28˚C, then separated by 
centrifugation at 4000 rotations per 
minute; supernatants were discarded and in 
the tests was added 5 ml of dissolvent for 
the extraction of triphenyl formazan; 
samples were centrifugated again andthe 
absorbance was readed 
spectrophotometrically at 540 nm; the 
color intensity is proportional with 
dehydrogenases activity. 
Dehydrogenase activities were expressed 
as μg formazan per gram fresh vegetal 
material[12]. 
 
3. Results and Discussion 
 
The dynamics of glucose dehydrogenase, 
isocitrate dehydrogenase, α-ketoglutarate 
dehydrogenase and malate dehydrogenase 
activities have been studied in healthy and 
curled leaves of peach cv. Springcrest and 
are presented in Figs. 1-4. 
The activity of glucose dehydrogenase at 
cv. Springcrest is presented in Fig. 1, from 
which it can be seen that in healthy leaves 
this enzyme had the highest value – 0,0640 
μg formazan/g mat. in the last stage (VII) 
and it was followed in decreasing order by 
the values: 0,0356 μg formazan/g mat. (II), 
0,0251 μg formazan/g mat. (IV), 0,0232 μg 
formazan/g mat. (VI), 0,0212 μg 
formazan/g mat. (III), 0,0182 μg 
formazan/g mat. (V), 0,0156 μg 
formazan/g mat. (I). 
In the leaves infected by Taphrina 
deformans, glucose dehydrogenase activity 
recorded the smallest value in the third 

stage of infection - 0,0146 μg formazan/g 
mat., followed in increasing order by the 
values: 0,0156 μg formazan/g mat. (IV), 
0,0166 μg formazan/g mat. (V), 0,0168 μg 
formazan/g mat. (I), 0,0193 μg formazan/g 
mat. (II), 0,0217 μg formazan/g mat. (VI), 
0,0830 μg formazan/g mat. (VII). 
The activity of glucose dehydrogenase in 
attacked leaves, recorded values higher 
than the control (enzyme activity in 
healthy leaves), in the first stage 
(D/H=1,0769) and in the last stage 
(D/H=1,2968); in stage II (D/H=0,5421), 
stage III (D/H=0,6886), stage IV 
(D/H=0,6215), stage V (D/H=0,9120) and 
stage VI (D/H=0,9353) glucose 
dehydrogenase activity in diseased leaves 
was smaller than the enzyme activity 
recorded in healthy ones.  
Glucose dehydrogenase has an important 
role during fungal attack on the host plant, 
it can reduce quinones and phenoxy 
radicals and is able to neutralize the action 
of host plant peroxidases and 
polyphenoloxidase, which are used by 
plants to block the fungal attack [13]. 
Glucose dehydrogenase activity recordet at 
cv. Springcrestwas higher in diseased 
leaves at the begining and at the end of 
fungal attack; at the other dates of the 
determinations glucose dehydrogenase 
activity was higher in healthy leaves when 
compared with the activity from attacked 
peach leaves; the results obtained in this 
study indicated that Taphrina deformans 
was not able to produce high amounts of 
glucose dehydrogenase and to stop the 
action of the enzymes responsible for plant 
protection against the oxidative stress 
caused by fungus attack; these results are 
in opposition with those mentionated in 
literature, which say that in injured plants 
the enzymes from pentose phosphate 
pathway are increasing their activity [14]. 

 
 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

138 
 

 
Figure 1 The influence of Taphrina deformans Berk. (Tul.) attack on the dynamics of glucose 

dehydrogenase activity
 

 
In Fig. 2 are presented the results 
concerning the isocitrate dehydrogenase 
activity in healthy and in infected leaves 
by Taphrina deformans in cv.Springcrest. 
In healthy leaves, isocitrate dehydrogenase 
activity recorded the next values, presented 
in decreasing order: 0,0649 μg formazan/g 
mat. (I), 0,0514 μg formazan/g mat. (VII), 
0,0368 μg formazan/g mat. (V), 0,0317 μg 
formazan/g mat. (VI), 0,0268 μg 
formazan/g mat. (IV), 0,0238 μg 
formazan/g mat. (III) and 0,0157 μg 
formazan/g mat. (II). Isocitrate 
dehydrogenase activity in healthy peach 
leaves, had the highest value at the 
begining of the fungus attack and the 
smallest value of it’s activity was recorded 
in stage II. 
In diseased leaves the activity of isocitrate 
dehydrogenase had the highest value– 
0,0546 μg formazan/g mat. in the last stage 
(VII) and was followed in decreasing order 
by the values: 0,0512 μg formazan/g mat. 
(IV), 0,0455 μg formazan/g mat. (V), 
0,0447 μg formazan/g mat. (VI), 0,0239 μg 
formazan/g mat. (I), 0,0159 μg formazan/g 
mat. (II), 0,0138 μg formazan/g mat. (III). 
The activity of isocitrate dehydrogenase in 
the leaves infected by the fungus Taphrina 

deformans had smaller values in compare 
with those recorded in healthy ones at 
stages I (D/H=0,3682) and III 
(D/H=0,5798); at stages II (D/H=1,0127), 
IV (D/H=1,9104), V (D/H=1,2364), VI 
(D/H=1,4100) and VII (D/H=1,0622) the 
isocitrate dehydrogenase activity from 
diseased leaves was higher than the 
activity recorded in healthy leaves.  
Isocitrate dehydrogenase activity is 
increasing in the leaves naturaly infected 
by Taphrina deformans as the disease 
simptoms develops, this enzymes is 
provideing the substratum necessary for α-
ketoglutatate dehydrogenase activity, 
which recorded the same dymanic in it’s 
activity. Isocitrate dehydrogenase is the 
enzyme that reflects the increased 
respiratory rate from diseased peach 
leaves. 
The enhanced isocitrate dehydrogenase 
activity in the leaves infected by Taphrina 
deformans correlatd with a low 
photsynthesis activity [15] could be due to 
the synthesis of oxaloacetic acid by 
phosphoenolpyruvate carboxylase in the 
cytosol with subsequent transport into 
mitochondria where it serves as substratum 
for isocitrate dehydrogenaseactivity [16]. 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

139 
 

 

 
Figure 2 The influence of Taphrina deformansBerk. (Tul.) attack on the dynamics of isocitrate 

dehydrogenase activity  
 

In Fig. 3 are presented the results 
concerning the activity of α-ketoglutatate 
dehydrogenase from which it can bee seen 
that the highest value of this enzyme 
activity, in non-infected leaves, was 
registered in the last stage (VII) - 0,0813 
μg formazan/g mat. and it was followed in 
decreasing order by next values: 0,0376 μg 
formazan/g mat. (IV), 0,0359 μg 
formazan/g mat. (VI), 0,0188 μg 
formazan/g mat. (III), 0,0183 μg 
formazan/g mat. (II), 0,0162 μg 
formazan/g mat. (V), 0,0148 μg 
formazan/g mat. (I). 
In diseased leaves were recorded the 
following values of α-ketoglutatate 
dehydrogenase activity: 0,1055 μg 
formazan/g mat. (VII), 0,0698 μg 
formazan/g mat. (IV), 0,0587 μg 
formazan/g mat. (VI), 0,0434 μg 
formazan/g mat. (I), 0,0377 μg formazan/g 
mat. (V), 0,0185 μg formazan/g mat. (II), 
0,0153 μg formazan/g mat. (III). 
The activity of α-ketoglutatate 
dehydrogenase had higher values in 
diseased leaves when compared with the 
enzyme activity from the healthy ones in 
the stages: I (D/H=2,9324), II 

(D/H=1,0109), IV (D/H=1,8563), V 
(D/H=2,3271), VI (D/H=1,6350), VII 
(D/H=1,2976); in stage III (D/H=0,8138) 
this dehydrogenase activity recorded a 
decreasing in its activity, which was higher 
in healthy leaves. This dehydrogenase 
activity is increasing in the same time with 
the disease development. α-ketoglutatate 
dehydrogenase it is found in it’s soluble 
form in the mithocondrial matrix and it is 
considered one of the main center able to 
generate reactive oxygen species [17] in 
response to biotic stress caused by the 
pathogen attack. 
The increased α-ketoglutatate 
dehydrogenase activity from infected 
leaves suggest an increase in respiratory 
rate, dependent of the age of the leaves and 
fungus, and an intense activity of the 
enzymes from the antioxidant defense line, 
knowing that a high metabolic rate is 
followed by the increase of oxidative stress 
markers that are responsible for the aging 
of mitochondria, which are the main 
source of reactive oxygen species [18] due 
to multiple reactions that transfer electrons. 
The decreased α-ketoglutatate 
dehydrogenase activity recorded at III in 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

140 
 

diseased leaves could be due to the 
influence of reactive oxygen species, this 
enzyme in known to be one of the major 
target enzyme of this radicals, when 
inhibition of this enzyme take place and 

this limits the NADH availability and, as a 
result, the respiratory function of 
mitochondria [8, 19, 20, 21].  
 

 

 
3 The influence of Taphrina deformans Berk. (Tul.) attack on the dynamics of

α-ketoglutatate dehydrogenase activity 
 
 

The last stage in the Krebs cycle, in which 
L malate is oxidize to oxaloacetate is 
catalysed by the malate dehydrogenase. 
The activity of malate dehydrogenase (Fig. 
4), in healthy leaves had the smallest value 
– 0,0214 μg formazan/g mat. in the first 
stage of the determinations and it was 
followeed in increasing order by the next 
values: 0,0246 μg formazan/g mat. (III), 
0,0293 μg formazan/g mat. (VI), 0,0333 μg 
formazan/g mat. (V), 0,0352 μg 
formazan/g mat. (IV), 0,0428 μg 
formazan/g mat. (II) and 0,1069 μg 
formazan/g mat. (VII). 
In the leaves attacked by the fungus 
Taphrina deformans, malate 
dehydrogenase activity had the highest 
value – 0,0967 μg formazan/g mat. in the 
final stage of the attack (VII) and it was 
followeed in decreasing order by the 
values: 0,0512 μg formazan/g mat. (IV), 
0,0492 μg formazan/g mat. (VI), 0,0221 μg 
formazan/g mat. (II), 0,0216 μg 

formazan/g mat. (V), 0,0127 μg 
formazan/g mat. (I), 0,0045 μg formazan/g 
mat. (III). 
Malate dehydrogenase activityat peach cv. 
Springcrest recorded smaller values in 
diseased leaves in compare with the 
control in stages: I (D/H=0,5934), II 
(D/H=0,5163), III (D/H=0,1829), V 
(D/H=0,6486), VII (D/H=0,9045); in 
stages IV (D/H=1,4545) and VI 
(D/H=1,6791), this enzyme activity 
recorded higher values in leaves infected 
by the pathogenic fungus than the activity 
recorded in healthy leaves at the same 
dates.  
Malate dehydrogenase activity recorded, in 
general, smaller values in curled leaves 
comparative with the values recorded in 
control, these results are similar with those 
presented in literature at Nicotiana 
tabacum plants infected by viruses, where 
it was observed a decrease of malate 
dehydrogenase activity in diseased plants 



Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

141 
 

[22]. The decreased malate dehydrogenase 
activity from diseased leaves, can be 
correlated with the big amount of oxalate 
which is known to inhibit this enzyme 
activity [23]. 

The results obtained in this study show that 
the infection of peach leaves with 
Taphrina deformans, is followed by an 
enhancement of the activity of the enzymes 
of mitochondrial resiration except malate 
dehydrogenase activity. 

 

 
Figure 4 The influence of Taphrina deformans Berk. (Tul.) attack on the dynamics of 

malate dehydrogenase activity 
 

 
4. Conclusions 
 
Glucose dehidrogenase activity was 
smaller in diseased leaves, these results 
suggest that the host plant tissues were 
able to mobilize theirs defensive 
mechanisms against Taphrina deformans 
and to limit its attack. 
Isocitrate dehydrogenase and α-
ketoglutatate dehydrogenase activities 
recorded the same dynamics and were,in 
general, higher in the leaves infected by 
Taphrina deformans, than the activity 
recorded in healthy leaves. 
Malate dehydrogenase activity recorded 
specific variations from one date to 
another, but the enzyme activity was in 
general, smaller in diseased leaves. 
The results obtained in this study suggest 
that these dehydrogenases play important 
roles in defence machanisms against peach 
leaf curl infection; these reflects the ability 

of host plant to moblize its defensive 
enzymes and to limit the fungus attack and 
the damages produced by infection. 
 
5. References 
 
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Food and Environment Safety - Journal of Faculty of Food Engineering, Ştefan cel Mare University - Suceava 
Volume XII, Issue 2 – 2013 

 

 
Rodica CIOBANU, Changes of some dehydrogenase activities in the leaves of peach cultivar springcrest naturally infected 
with the fungus taphrina deformans, Food and Environment Safety, Volume XII, Issue 2 – 2013, pag.  135 - 142 

142 
 

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