Malgorzata R Cyran

Prof. Dr. Malgorzata R Cyran

orcid

Research Focus & Metrics

Academic Career Length

24Years (2003-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
17 June 2003 in Journal of Agricultural and Food Chemistry
Verified
Journal Article
Closed access
MCMalgorzata R Cyran
Malgorzata R Cyran
CCChristophe Courtin
Christophe Courtin
JDJan A. Delcour
Jan A. Delcour


17 February 2007 in Journal of Agricultural and Food Chemistry
Verified
Journal Article
Closed access
MCMalgorzata R Cyran
Malgorzata R Cyran
LSLuc Saulnier
Luc Saulnier

27 October 2010 in Journal of the Science of Food and Agriculture
Verified
Journal Article
Closed access
PDF file
MCMalgorzata R Cyran
Malgorzata R Cyran
ACAlicja Ceglinska
Alicja Ceglinska


1 February 2014 in Food Chemistry
Verified
Journal Article
Open access
MCMalgorzata R Cyran
Malgorzata R Cyran
WDWioletta Monika Dynkowska
Wioletta Monika Dynkowska
Insight into solubilisation mechanisms of rye arabinoxylans during breadmaking is important for understanding the biochemical processes that affect bread attributes. Purified ethanol precipitated water-extractable arabinoxylans (WE-AX) and residual unextractable counterparts (WU-AX) were isolated from rye flours and resulting breads. While the endosperm flours had lower endoxylanase activities and higher arabinose-to-xylose ratios of WU-AX than those of corresponding wholemeals, there were not any significant differences between them in the mean amounts of WU-AX hydrolysed during breadmaking. Nevertheless, they were highly affected by rye cultivar used for breadmaking. On average, 42% and 36% of WU-AX were recovered in bread WE-AX fraction, causing its 11% and 8% increase, respectively for endosperm and wholemeal breads. Bread WE-AX, however, had lower molecular weights than those of starting flours, implying chains depolymerisation. Degree of AX solubilisation depends mainly on rye genotype used, determining combined effect of enzymatic and acid hydrolyses, associations and fine structure of AX.