Tags

Type your tag names separated by a space and hit enter

Digestive proteinase activity of the Khapra beetle, Trogoderma granarium Everts (Coleoptera: Dermestidae).
Commun Agric Appl Biol Sci. 2005; 70(4):879-82.CA

Abstract

The khapra beetle, Trogoderma granarium, is one of the most important stored product pests worldwide. A study of digestive proteinases in T. granarium was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. The pH of guts was determined by addition of pH indicator solutions to broken open gut regions. The last instar larvae were dissected in cold distilled water and the whole guts were cleaned from adhering unwanted tissues. The pooled gut homogenates were centrifuged and the supernatants were used in the subsequent enzyme assay. Total proteinases activity of the gut homogenates was determined using the protein substrate azocasein. Optimal azocasein hydrolysis by luminal proteinases of the larvae of T. granarium was highly alkaline in pH 10-10.5, although the pH of luminal contents was slightly acidic (pH 6.5). The extract showed the highest activity at 55 degrees C (pH 6.5), 45 degrees C (pH 8) and 30 degrees C (pH 10). The proteolytic activity was strongly inhibited in the presence of phenylmethylsulphonyl fluoride (82.33+/-4.37% inhibition). This inhibition was decreased with increasing of the pH of assay incubating medium. N-p-tosyl-L-lysine chloromethyl ketone (51.6+/-3.3% inhibition) and N-tosyl-L-phenylalanine chloromethyl ketone (27.23+/-4.37 % inhibition) showed inhibitory effect on proteolysis. Addition of thiol activators dithiothreitol and L-cysteine had not enhanced azocaseinolytic activity. The data suggest that protein digestion in the larvae of T. granarium is primarily dependent on serine proteinases; trypsin- and chymotrypsin-like proteinases.

Authors+Show Affiliations

Department of Plant protection, College of Agriculture, University of Tehran, Karaj, Iran.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16628932

Citation

Naveh, V Hosseini, et al. "Digestive Proteinase Activity of the Khapra Beetle, Trogoderma Granarium Everts (Coleoptera: Dermestidae)." Communications in Agricultural and Applied Biological Sciences, vol. 70, no. 4, 2005, pp. 879-82.
Naveh VH, Bandani AR, Azmayeshfard P, et al. Digestive proteinase activity of the Khapra beetle, Trogoderma granarium Everts (Coleoptera: Dermestidae). Commun Agric Appl Biol Sci. 2005;70(4):879-82.
Naveh, V. H., Bandani, A. R., Azmayeshfard, P., & Hosseinkhani, S. (2005). Digestive proteinase activity of the Khapra beetle, Trogoderma granarium Everts (Coleoptera: Dermestidae). Communications in Agricultural and Applied Biological Sciences, 70(4), 879-82.
Naveh VH, et al. Digestive Proteinase Activity of the Khapra Beetle, Trogoderma Granarium Everts (Coleoptera: Dermestidae). Commun Agric Appl Biol Sci. 2005;70(4):879-82. PubMed PMID: 16628932.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Digestive proteinase activity of the Khapra beetle, Trogoderma granarium Everts (Coleoptera: Dermestidae). AU - Naveh,V Hosseini, AU - Bandani,A R, AU - Azmayeshfard,P, AU - Hosseinkhani,S, PY - 2006/4/25/pubmed PY - 2006/7/13/medline PY - 2006/4/25/entrez SP - 879 EP - 82 JF - Communications in agricultural and applied biological sciences JO - Commun Agric Appl Biol Sci VL - 70 IS - 4 N2 - The khapra beetle, Trogoderma granarium, is one of the most important stored product pests worldwide. A study of digestive proteinases in T. granarium was performed to identify potential targets for proteinaceous biopesticides, such as proteinase inhibitors. The pH of guts was determined by addition of pH indicator solutions to broken open gut regions. The last instar larvae were dissected in cold distilled water and the whole guts were cleaned from adhering unwanted tissues. The pooled gut homogenates were centrifuged and the supernatants were used in the subsequent enzyme assay. Total proteinases activity of the gut homogenates was determined using the protein substrate azocasein. Optimal azocasein hydrolysis by luminal proteinases of the larvae of T. granarium was highly alkaline in pH 10-10.5, although the pH of luminal contents was slightly acidic (pH 6.5). The extract showed the highest activity at 55 degrees C (pH 6.5), 45 degrees C (pH 8) and 30 degrees C (pH 10). The proteolytic activity was strongly inhibited in the presence of phenylmethylsulphonyl fluoride (82.33+/-4.37% inhibition). This inhibition was decreased with increasing of the pH of assay incubating medium. N-p-tosyl-L-lysine chloromethyl ketone (51.6+/-3.3% inhibition) and N-tosyl-L-phenylalanine chloromethyl ketone (27.23+/-4.37 % inhibition) showed inhibitory effect on proteolysis. Addition of thiol activators dithiothreitol and L-cysteine had not enhanced azocaseinolytic activity. The data suggest that protein digestion in the larvae of T. granarium is primarily dependent on serine proteinases; trypsin- and chymotrypsin-like proteinases. SN - 1379-1176 UR - https://www.unboundmedicine.com/medline/citation/16628932/Digestive_proteinase_activity_of_the_Khapra_beetle_Trogoderma_granarium_Everts__Coleoptera:_Dermestidae__ DB - PRIME DP - Unbound Medicine ER -