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Organic production systems in Northern highbush blueberries Organic Eprints
Caspersen, S.; Svensson, B.; Khalil, S.; Asp, H..
The production of highbush blueberries is increasing worldwide. Organic production of blueberries in Sweden is presently very limited but is expected to have a great potential to expand as the berries are popular and have a good shelf life. The fact that blueberries require acid soils raises several questions concerning suitable substrates in combination with mycorrhizal inoculation and fertilization in organic production systems. Field and pot experiments have been established during 2011 and 2012 with the aim of developing a sustainable production system for high quality organic blueberries. After the second experimental year, total fruit yields were similar for plants grown in a plastic tunnel and in the open field. Yields were not affected by the...
Tipo: Conference paper, poster, etc. Palavras-chave: Greenhouses and coverings; Fruit and berries.
Ano: 2013 URL: http://orgprints.org/24582/1/24582.pdf
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Tyrosine 105 and threonine 212 at outermost substrate binding subsites –6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1 Inra
Bak-Jensen, K.S.; André, G.; Gottschalk, T.E.; Paës, G.; Tran, V.; Svensson, B..
The role in activity of outer regions in the substrate binding cleft in α-amylases is illustrated by mutational analysis of Tyr105 and Thr212 localized at subsites –6 and +4 (substrate cleavage occurs between subsites –1 and +1) in barley α-amylase 1 (AMY1). Tyr105 is conserved in plant α-amylases whereas Thr212 varies in these and related enzymes. Compared with wild-type AMY1, the subsite –6 mutant Y105A has 140, 15, and <1% activity (kcat/Km) on starch, amylose DP17, and 2-chloro-4-nitrophenyl β-d-maltoheptaoside, whereas T212Y at subsite +4 has 32, 370, and 90% activity, respectively. Thus engineering of aromatic stacking interactions at the ends of the 10-subsite long binding cleft affects activity very differently, dependent on the substrate. Y105A...
Tipo: Journal Article Palavras-chave: LIAISON ENZYME SUBSTRAT; ARRIMAGE; SITE DE LIAISON; MODÉLISATION MOLÉCULAIRE.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0600012057111406&uri=/notices/prodinra1/2010/11/
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