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Your search keyword '"Brinch-Pedersen, Henrik"' showing total 5 results
Start Over Author "Brinch-Pedersen, Henrik" Journal journal of agricultural and food chemistry
5 results on '"Brinch-Pedersen, Henrik"'

2. Superior Growth Rates in Broilers Fed Wheat with Low In Vitro Feed-Xylanase Inhibition

Author

Krogh Madsen, Claus, Pettersson, Dan, Hjortshøj, Rasmus, Katholm, Anders, and Brinch-Pedersen, Henrik

Abstract

Grain-batch variation in xylanase-inhibitor levels may account for variations in the efficacy of feed xylanase supplementation. This would make inhibition an important quality parameter in the routine analysis of feedstuffs. Two analytical procedures for testing feedstuffs against specific xylanases were researched: the high-throughput viscosity-pressure assay (ViPr) and the extraction-free remazol-brilliant-blue–beechwood-xylan (RBBX) assay. Thirty-two wheat cultivars were analyzed for inhibition of a commercial xylanase, Ronozyme WX. Four cultivars were selected for a feeding experiment in which the growth of 1440 broilers from ages 7–33 days was monitored. The treatments resulted up to 7 % difference (day 14) in broiler weight . The cultivar choice had an effect throughout the experiment (p< 0.05). The performance ranking of the treatments corresponded better to xylanase inhibition than to crude-protein content or nonstarch-polysaccharide content. Wheat-grain xylanase-inhibitor content is therefore a highly relevant quality parameter when broiler diets are supplemented with feed xylanase.

Published
2024
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5. Heat-stable phytases in transgenic wheat (Triticum aestivum L.): deposition pattern, thermostability, and phytate hydrolysis.

Author

Brinch-Pedersen H, Hatzack F, Stöger E, Arcalis E, Pontopidan K, and Holm PB

Subjects
6-Phytase analysis, 6-Phytase metabolism, Aspergillus fumigatus enzymology, Aspergillus fumigatus genetics, Enzyme Stability, Gene Expression, Hot Temperature, Hydrolysis, Inositol Phosphates metabolism, Protein Denaturation, Triticum genetics, 6-Phytase genetics, Phytic Acid metabolism, Plants, Genetically Modified enzymology, Triticum enzymology
Abstract

The present paper addresses the question of thermotolerance of in planta synthesized heterologous enzymes using phytase as a model. Two individual transgenic wheat materials expressing an Aspergillus fumigatus phytase with a low denaturation temperature (62.5 degrees C) but a high refolding capacity, and a rationally designed consensus phytase engineered to a high denaturation temperature (89.3 degrees C), were evaluated. High levels of endosperm specific expression were ensured by the wheat high molecular weight glutenin 1DX5 promoter. Immunodetection at the light and electron microscopical level shows unequivocally that the heterologous phytase is deposited in the vacuole, albeit that the transformation constructs were designed for secretion to the apoplast. Evaluation of heat stability properties and kinetic properties unraveled that, under these deposition conditions, heat stability based on high unfolding temperature is superior to high refolding capacity and represents a realistic strategy for improving phosphate and mineral bioavailability in cereal-based feed and food.

Published
2006
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