ISSN:
1573-5109
Keywords:
α-amylase
;
β-amylase
;
barley
;
β-glucanase
;
grain residual proteins
;
grain size
;
hordeins
;
Hordeum vulgare
;
landraces
Source:
Springer Online Journal Archives 1860-2000
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Notes:
Abstract Thirty-two unimproved landraces of barley ( Hordeum vulgare L.) based on single plant selections in SE Finland were studied. Some of the lines still had ancient features, e.g., rachis brittleness in the tip of the spike. The lines showed 17 different and 16 unique hordein patterns and three lines showed more than one pattern, suggesting heterozygosity, and six different residual grain protein patterns. The three enzyme activities (α-amylase, β-amylase and β-glucanase) of grains germinated aseptically for 120 h were determined. The average activity levels were high compared with a standard of five global barleys and with those determined previously in wild barley (H. vulgare ssp. spontaneum (Koch) Archers et Graebn.) grown in Finland. The ssp. spontaneum sample of 257 accessions showed significantly (P〈0.001) less variation in β-amylase and significantly (P〈0.001) lower mean activity of all three enzymes. The high variation of these chemotypes indicates great potential variation of possible use by breeders has been lost by the disappearance and displacement of local barleys with commercial cultivars since 1950 in Finland before which barley cultivation and adaptation to the local environment had occurred over more than 3000 years. Selection for currently preferable plant characteristics in the descendants of the cross of HA52 (a landrace selection) × Adorra discriminated the hordein pattern of HA52 not being directly selected. The best landraces outyield the standard cultivars especially when there was no lodging. Top yield and small grains appeared to be associated characteristics under the environmental selection pressure, conflicting with the man-made regulations of the EU.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008605307102
