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Bernard Quemener

Researcher at Institut national de la recherche agronomique

Publications -  61
Citations -  3164

Bernard Quemener is an academic researcher from Institut national de la recherche agronomique. The author has contributed to research in topics: Xyloglucan & Hydrolysis. The author has an hindex of 32, co-authored 61 publications receiving 2862 citations.

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GDP‐d‐mannose 3,5‐epimerase (GME) plays a key role at the intersection of ascorbate and non‐cellulosic cell‐wall biosynthesis in tomato

TL;DR: Using transgenic tomato lines that were RNAi-silenced for GME, it is confirmed that GME does indeed play a key role in the regulation of ascorbate biosynthesis in plants, a fact that helps to explain the common factors in seemingly unrelated traits such as fruit firmness and asCorbate content.
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Determination of the degrees of methylation and acetylation of pectins using a C18 column and internal standards

TL;DR: In this article, an improved hplc method for the simultaneous determination of the degrees of methylation and acetylation of pectins has been developed, which involves saponification in heterogeneous medium followed by the separation of methanol, acetic acid and internal standard on a C18 column and quantification by refractometry.
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Effects of xylanase and beta-glucanase addition on performance, nutrient digestibility and physico chemical conditions in the small intestine contents and caecal microflora of broiler chickens fed a wheat and barley based diet

TL;DR: The addition of xylanase and β-glucanase to the wheat and bar- ley-based diet significantly reduced the viscosity of the small intestine contents and improved the weight gain, feed intake and feed conversion ratio.
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Sugar determination in ulvans by a chemical-enzymatic method coupled to high performance anion exchange chromatography

TL;DR: In this article, the sugar determination of ulvans, the water-soluble polysaccharides from Ulva sp and Enteromorpha sp, was optimized by combining partial acid prehydrolysis (2 mol L-1 trifluoroacetic acid, 120°C) with enzymic hydrolysis with β-D-glucuronidase.