Characterization and partial purification of proteinases from the highly 
alkaline midgut of the humivorous larvae of Pachnoda ephippiata (Coleoptera: 
Scarabaeidae)

Zhang, H.; Brune, A.

doi:10.1016/j.soilbio.2003.10.021

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Characterization and partial purification of proteinases from the highly alkaline midgut of the humivorous larvae of Pachnoda ephippiata (Coleoptera: Scarabaeidae)

Zhang, H., & Brune, A. (2004). Characterization and partial purification of proteinases from the highly alkaline midgut of the humivorous larvae of Pachnoda ephippiata (Coleoptera: Scarabaeidae). Soil Biology & Biochemistry, 36(3), 435-442. doi:10.1016/j.soilbio.2003.10.021.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-C92C-6 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-5B94-6

Genre: Journal Article

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Creators:
Zhang, H., Author
Brune, A.¹, Author

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1Department of Biology, Microbial Ecology, University of Konstanz, Germany, ou_persistent22

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Free keywords: SOIL-FEEDING TERMITES, HUMIC MODEL COMPOUNDS, COSTELYTRA-ZEALANDICA, DIGESTIVE ENZYMES, AMINO-ACIDS, GUT, INHIBITORS, PROTEASES, INSECTS, MINERALIZATION

Abstract: Proteinases in the humus-feeding larva of Pachnoda ephippiata were partially purified and characterized. Proteinase activity from the midgut was alkali-stable and its pH optimum for activity was about pH 12. Nine proteolytic bands were visible on zymogram gels containing gelatin; one band of 19 kDa was dominant. P. ephippiata mainly employed serine proteinases for digestive proteolysis. The combination of strong midgut alkalinity and midgut proteinases with pronounced alkali stability, a high proteolytic activity on model humic acids, and a large tolerance to high humic acid concentrations would enable the P. ephippiata to gain nutrients from soil by digesting the proteinaceous component of soil humic substances.

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Dates: Date issued: 2004-05

Publication Status: Issued

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Rev. Type: Peer

Identifiers: eDoc: 124196
DOI: 10.1016/j.soilbio.2003.10.021

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Title: Soil Biology & Biochemistry

Source Genre: Journal

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Pages: - Volume / Issue: 36 (3) Sequence Number: - Start / End Page: 435 - 442 Identifier: -