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Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae)

Published online by Cambridge University Press:  09 March 2007

B. Oppert ,
K. Hartzer  and
M. Zuercher
B. Oppert*
Affiliation:
USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA
K. Hartzer
Affiliation:
Department of Entomology, Kansas State University, Waters Hall, Manhattan, KS 66506, USA
M. Zuercher
Affiliation:
USDA ARS Grain Marketing and Production Research Center, 1515 College Avenue, Manhattan, KS 66502, USA
*
*Fax: 785 537 5584 E-mail: bso@ksu.edu
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Abstract

The cigarette beetle, Lasioderma serricorne (Fabricius), is a common pest of stored foods. A study of digestive proteinases in L. serricorne was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. Optimal casein hydrolysis by luminal proteinases of L. serricorne was in pH 8.5–9.0 buffers, although the pH of luminal contents was slightly acidic. Results from substrate and inhibitor analyses indicated that the primary digestive proteinases were serine proteinases. The most effective inhibitors of caseinolytic hydrolysis were from soybean (both Bowman Birk and Kunitz), with some inhibition by chymostatin, N-TOSYL-L-phenylalanine chloromethyl ketone, and leupeptin. Casein zymogram analysis identified at least eight proteolytic activities. Activity blot analyses indicated one major proteinase activity that hydrolysed the trypsin substrate N-α-benzoyl-L-arginine ρ-nitroanilide, and three major proteinase activities that hydrolysed the chymotrypsin substrate N-succinyl ala-ala-pro-phe ρ-nitroanilide. The absence of cysteine, aspartic, and metallo proteinases in L. serricorne digestion was evidenced by the lack of activation by thiol reagents, alkaline pH optima, and the results from class-specific proteinase inhibitors. The data suggest that protein digestion in L. serricorne is primarily dependent on trypsin- and chymotrypsin-like proteinases.

Information

Type
Research Article
Information
Bulletin of Entomological Research , Volume 92 , Issue 4 , August 2002 , pp. 331 - 336
Copyright
Copyright © Cambridge University Press 2002

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