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Preliminary characterization of laminarinase from Trichoderma longibrachiatum

✍ Scribed by A. Sharma; Nakas J.P.

Book ID
103524997
Publisher
Elsevier Science
Year
1987
Tongue
English
Weight
420 KB
Volume
9
Category
Article
ISSN
0141-0229

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πŸ“œ SIMILAR VOLUMES

Solution scattering studies of conformat
Solution scattering studies of conformation stability of xylanase XYNII from Trichoderma longibrachiatum
✍ Maciej Kozak πŸ“‚ Article πŸ“… 2006 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 288 KB

## Abstract Xylanase (__endo__‐1,4‐β‐xylanase; EC 3.2.1.8) is an enzyme that catalyzes the hydrolysis reaction of xylan. The structure of the xylanase II (XYNII) molecule from __Trichoderma longibrachoatum__ (formerly __Trichoderma reesei__) in a solution and at different pH values has been studied

Synchrotron radiation small angle scatte
Synchrotron radiation small angle scattering studies of thermal stability of xylanase XYNII from Trichoderma longibrachiatum
✍ Maciej Kozak πŸ“‚ Article πŸ“… 2006 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 268 KB

## Abstract Xylanase XYNII from __Trichoderma longibrachiatum__ is a small protein of the molecular weight 21 kDa, belonging to the family 11 of glycosyl hydrolases, which catalyses hydrolysis of xylan. This article reports thermal stability study of xylanase XYN II conformation in the temperature

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Using barium ions for heavy-atom derivatization and phasing of xylanase II from Trichoderma longibrachiatum
✍ Moiseeva, Natalia ;Allaire, Marc πŸ“‚ Article πŸ“… 2007 πŸ› International Union of Crystallography 🌐 English βš– 468 KB

This paper describes the use of barium chloride to produce a heavy-atom derivative of xylanase II crystals from Trichoderma longibrachiatum, which was obtained either by cocrystallization or soaking. SAD phasing led to interpretable electron-density maps that allowed unambiguous chain tracing. In th