After the ALAMY_7
Introduction
Programme
Committee
Topics
and
Sessions
Invited
Speakers
Selected Oral Talks
Poster board size
Final programme
Important
dates
Sponsors
Registration
and Abstracts
Fees
and Payments
Conference buses
Internet in the Castle
Weather in Smolenice
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The
journal "Amylase" |
Selected
Oral Talks
In
addition to Invited Lectures, the
following Oral Talks have already been confirmed.
The list is not complete; up to 20 Oral Talks can be selected from
submitted Abstracts.
Birte
Svensson (Department
of Biotechnology and Biomedicine, Technical
University of Denmark, Kgs. Lyngby, Denmark): Surface binding sites
and starch binding domains in enzymes involved in starch biosynthesis
Marcelo Guerin (Structural Biology Unit - CIC bioGUNE, Technological Park of Bizkaia, Derio, Vizcaya,
Spain): Structural
basis of glycogen biosynthesis
regulation in bacteria
Matthew S.
Gentry (Department of Molecular and
Cellular
Biochemistry, University of Kentucky, Lexington, KY, USA): Targeting pathogenic
Lafora bodies in Lafora disease using an antibody-amylase fusion
Michiyo Yanase (Institute
of Health
Sciences, Ezaki Glico Co., Ltd., Osaka, Japan): Enzymatic
synthesis of glucan dendrimer for the drug carrier and its application
Eiji Suzuki (Department of Biological Production, Faculty
of
Bioresource Sciences, Akita Prefectural University, Akita, Japan): Differential
binding of polysaccharides at surface binding sites of branching
enzymes from amylopectin producing cyanobacteria
Marie Sophie Moeller (Department
of Biotechnology and Biomedicine, Technical
University of Denmark,
Kgs. Lyngby, Denmark): Selectivity
and regulation of barley limit dextrinase approached by
computational-guided and rational engineering
Purnananda
Guptasarma (Department of
Biological Sciences, Indian
Institute of Science Education and Research, Mohali, SAS Nagar,
Punjab, India): Exoamylases that also act as
disproportionating
glucanotransferases
Manon Molina (Laboratoire
Ingenierie des Systemes Biologiques et des
Procedes, Universite de Toulouse, Toulouse, France): Exploration of the molecular determinants
involved in alternansucrase specificity and polymerization
Darrell
Cockburn (Department
of Food Science, The Pennsylvania
State
University, University Park, PA, USA): Structure and characterization of the maltogenic
amylase Amy13B from Eubacterium rectale
Kuakarun Krusong (Department of Biochemistry, Faculty of
Science, Chulalongkorn
University, Bangkok, Thailand): Amylomaltase
and large-ring cyclodextrins
Maher
Abou
Hachem (Department
of Biotechnology and Biomedicine, Technical
University of Denmark, Kgs. Lyngby, Denmark): A new disproportionating enzyme defines a new
route of maltooligosaccharide metabolism in Lactobacillus
Xuewen
Zhang (Department
of Aquatic Biotechnology and Bioproduct Engineering, University
of Groningen, Groningen, The Netherlands): The roles of GH13 and GH57 glycogen branching enzymes
from Petrotoga mobilis SJ95
Jonathan Monroe (Department of Biology, James
Madison University, Harrisonburg, VA, USA):
Arabidopsis
beta-amylase2
(BAM2) is an unusual enzyme with a potentially unique
function
Matthias Thalmann (John Innes Centre, Norwich
Research Park,
Norwich, NR4 7UH, United Kingdom): The
evolution of the beta-amylase gene family in plants
Matthieu
Colpaert (University Lille, CNRS, Unité de
Glycobiologie Structurale et Fonctionnelle, Lille,
France): Both chlamydia-related bacteria, Estrella
lausannensis and Wadddlia chondrophila
synthesize glycogen particles via GlgE-pathway
Amanda Photenhauer (Department
of Microbiology & Immunology, University
of Michigan Medical School, Ann Arbor, MI, USA): CBM74-containing
proteins contribute to resistant starch breakdown in the human gut
Casper Wilkens (Department
of Biotechnology and Biomedicine, Technical
University of Denmark, Kgs. Lyngby, Denmark): Carbohydrate binding
module of family 48 does not only bind starch
Special ALAMY_7 Oral Talk - Lubica
Urbanikova (Laboratory of Protein
Evolution, Institute of Molecular Biology, Slovak Academy of Sciences,
Bratislava, Slovakia): Acetylesterases of the family CE16
– in silico analysis
and comparison with
related CAZy CE families and SGNH hydrolases
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