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Fractionation of digestive proteinases from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae and role in protein digestion.
Comp Biochem Physiol B Biochem Mol Biol. 2006 Oct; 145(2):138-46.CB

Abstract

Tenebrio molitor larval digestive proteinases were purified and characterized by gel filtration chromatography combined with activity electrophoresis. Cysteine proteinases, consisting of at least six distinct activities, were found in three chromatographic peaks in anterior and posterior midgut chromatographies. The major activity in the anterior midgut, peak cys II, consisted of cysteine proteinases with Mm of 23 kDa. The predominant peak in the posterior, cys I, was represented by 38 kDa proteinases. The activities of all cysteine proteinases were maximal in buffers from pH 5.0 to 7.0, with 80% stability at pH values from 4.0 to 7.0. In the conditions of the last third of the midgut, the activity and stability of cysteine proteinases was sharply decreased. Trypsin-like activity included a minor peak of "heavy" trypsins with Mm 59 kDa, located mainly in the anterior midgut. An in vitro study of the initial stages of digestion of the main dietary protein, oat 12S globulin, by anterior midgut proteinases revealed that hydrolysis occurred through the formation of intermediate high-Mm products, similar to those formed during oat seed germination. Cysteine proteinases from the cys III peak and heavy trypsins were capable of only limited proteolysis of the protein, whereas incubation with cys II proteinases resulted in substantial hydrolysis of the globulin.

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Authors+Show Affiliations

Vinokurov KS
Department of Entomology, Biological Faculty, Moscow State University, Moscow 119992, Russia.
Elpidina EN
No affiliation info available
Oppert B
No affiliation info available
Prabhakar S
No affiliation info available
Zhuzhikov DP
No affiliation info available
Dunaevsky YE
No affiliation info available
Belozersky MA
No affiliation info available

MeSH

AnimalsAvenaCysteine EndopeptidasesDigestionDigestive SystemHydrolysisInsect ProteinsLarvaPlant Proteins, DietaryTenebrio

Pub Type(s)

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

Language

eng

PubMed ID

16926103

Citation

Vinokurov, K S., et al. "Fractionation of Digestive Proteinases From Tenebrio Molitor (Coleoptera: Tenebrionidae) Larvae and Role in Protein Digestion." Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, vol. 145, no. 2, 2006, pp. 138-46.
Vinokurov KS, Elpidina EN, Oppert B, et al. Fractionation of digestive proteinases from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae and role in protein digestion. Comp Biochem Physiol B Biochem Mol Biol. 2006;145(2):138-46.
Vinokurov, K. S., Elpidina, E. N., Oppert, B., Prabhakar, S., Zhuzhikov, D. P., Dunaevsky, Y. E., & Belozersky, M. A. (2006). Fractionation of digestive proteinases from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae and role in protein digestion. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 145(2), 138-46.
Vinokurov KS, et al. Fractionation of Digestive Proteinases From Tenebrio Molitor (Coleoptera: Tenebrionidae) Larvae and Role in Protein Digestion. Comp Biochem Physiol B Biochem Mol Biol. 2006;145(2):138-46. PubMed PMID: 16926103.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Fractionation of digestive proteinases from Tenebrio molitor (Coleoptera: Tenebrionidae) larvae and role in protein digestion. AU - Vinokurov,K S, AU - Elpidina,E N, AU - Oppert,B, AU - Prabhakar,S, AU - Zhuzhikov,D P, AU - Dunaevsky,Y E, AU - Belozersky,M A, Y1 - 2006/05/23/ PY - 2005/12/22/received PY - 2006/05/15/revised PY - 2006/05/16/accepted PY - 2006/8/24/pubmed PY - 2007/7/26/medline PY - 2006/8/24/entrez SP - 138 EP - 46 JF - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology JO - Comp Biochem Physiol B Biochem Mol Biol VL - 145 IS - 2 N2 - Tenebrio molitor larval digestive proteinases were purified and characterized by gel filtration chromatography combined with activity electrophoresis. Cysteine proteinases, consisting of at least six distinct activities, were found in three chromatographic peaks in anterior and posterior midgut chromatographies. The major activity in the anterior midgut, peak cys II, consisted of cysteine proteinases with Mm of 23 kDa. The predominant peak in the posterior, cys I, was represented by 38 kDa proteinases. The activities of all cysteine proteinases were maximal in buffers from pH 5.0 to 7.0, with 80% stability at pH values from 4.0 to 7.0. In the conditions of the last third of the midgut, the activity and stability of cysteine proteinases was sharply decreased. Trypsin-like activity included a minor peak of "heavy" trypsins with Mm 59 kDa, located mainly in the anterior midgut. An in vitro study of the initial stages of digestion of the main dietary protein, oat 12S globulin, by anterior midgut proteinases revealed that hydrolysis occurred through the formation of intermediate high-Mm products, similar to those formed during oat seed germination. Cysteine proteinases from the cys III peak and heavy trypsins were capable of only limited proteolysis of the protein, whereas incubation with cys II proteinases resulted in substantial hydrolysis of the globulin. SN - 1096-4959 UR - https://www.unboundmedicine.com/medline/citation/16926103/Fractionation_of_digestive_proteinases_from_Tenebrio_molitor__Coleoptera:_Tenebrionidae__larvae_and_role_in_protein_digestion_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1096-4959(06)00132-1 DB - PRIME DP - Unbound Medicine ER -