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Cooperation of enzymes involved in carbohydrate digestion of Colorado potato beetle (Leptinotarsa decemlineata, Say)

Published online by Cambridge University Press:  11 April 2019

E. Szilágyi ,
C. Hámori ,
P. Bíró-Molnár ,
L. Kandra ,
J. Remenyik  and
G. Gyémánt Open the ORCID record for G. Gyémánt [Opens in a new window]
E. Szilágyi
Affiliation:
Institute of Food Technology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, H-4032 Debrecen, Hungary
C. Hámori
Affiliation:
Department of Inorganic and Analytical Chemistry, Faculty of Sciences and Technology, University of Debrecen, H-4032 Debrecen, Hungary
P. Bíró-Molnár
Affiliation:
Institute of Food Technology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, H-4032 Debrecen, Hungary
L. Kandra
Affiliation:
Institute of Food Technology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, H-4032 Debrecen, Hungary
J. Remenyik
Affiliation:
Institute of Food Technology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, H-4032 Debrecen, Hungary
G. Gyémánt*
Affiliation:
Department of Inorganic and Analytical Chemistry, Faculty of Sciences and Technology, University of Debrecen, H-4032 Debrecen, Hungary
*
*Author for correspondence Phone: 0036 52 518 660 Fax: +36 52 518660 E-mail: [email protected]
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Abstract

Colorado potato beetle (Leptinotarsa decemlineata, Say) is the main pest of Solanaceae and its survival is mainly dependent on the carbohydrate digestion. Characterizing the gut enzymes may help us with finding effective inhibitors for plant protection. Activity measurements revealed that gut extracts contain α- and β-glucosidase in addition to α-amylase. For larvae, amylase activity was detected only in gut saturated with nutrients. Leptinotarsa decemlineata α-amylase (LDAmy) had optimum pH of 6.0 and was active under 30–40°C temperature measured on a selective α-amylase substrate, 2-chloro-4-nitrophenyl-4-O-α-D-galactopyranosyl-maltoside. HPLC analysis demonstrated dimer, trimer, and tetramer reducing end amylolytic products from 2-chloro-4-nitrophenyl-maltoheptaoside substrate in similar ratio than that of during porcine pancreatic α-amylase (PPA) catalyzed hydrolysis. The 4,6-O-benzylidene-modified substrate (BzG7PNP) is very stable toward hydrolysis by exo-glycosidases, therefore is very useful to monitor the digestion catalyzed by α-amylases exclusively. Similarly to PPA active site, three glycon and two aglycon binding sites are suggested for LDAmy based on the pattern of early hydrolysis products of BzG7PNP. The observed similarity between LDAmy and PPA raises the possibility of using known inhibitors of mammalian α-amylases to protect the potato plant from attack of Colorado potato beetle.

Keywords

Colorado potato beetlecarbohydrate digestiongut enzymesalpha-amylaseHPLCchromogen substrates
Type
Research Paper
Information
Bulletin of Entomological Research , Volume 109 , Issue 5 , October 2019 , pp. 695 - 700
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Copyright
Copyright © Cambridge University Press 2019 

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