Phenotypic Variation for Diastatic Power, β‐Amylase Activity, and β‐Amylase Thermostability vs. Allelic Variation at the <i>Bmy1</i> Locus in a Sample of North American Barley Germplasm

Filichkin, Tanya; Vinje, Marcus A.; Budde, Allen D.; Corey, Ann; Duke, Stanley H.; Gallagher, L. W.; Helgesson, J.; Henson, Cynthia A.; Obert, D. E.; Ohm, Jae‐Bom; Petrie, S. E.; Ross, Andrew S.; Hayes, Patrick

doi:10.2135/cropsci2009.04.0231

Cited by 29 publications

(21 citation statements)

References 45 publications

(137 reference statements)

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“…Furthermore, Duke and Henson (2009a) could not discern any apparent differences in β-amylase activity in elite two-and six-row barley cultivars (i.e., Bmy1.b and Bmy1.a intron III alleles). In a recent North American spring barley breeding trial, an abundant amount of variation in DP, β-amylase activity, and thermostability was observed despite the parents containing the exact same Bmy1 intron III allele, indicating the genetic basis of the variation did not reside inside the third intron (Filichkin et al 2010). These discrepancies exemplify the need for ensuring that identified polymorphisms serve a functional purpose as a marker by demonstrating without a doubt to have strong associations with the trait of interest in the targeted germplasm before using them in a breeding program.…”

Section: Resultsmentioning

confidence: 99%

Utilization of Different Bmy1 Intron III Alleles for Predicting β-Amylase Activity and Thermostability in Wild and Cultivated Barley

2010

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The third intron of barley (Hordeum vulgare L.) β-amylase 1 (Bmy1) is extremely polymorphic. The use of specific insertion/deletions (indels) in the third intron as markers for cultivar development has been recommended based on associations with β-amylase activity and thermostability. The third intron of Bmy1 in 40 barley genotypes was sequenced and aligned with 15 Bmy1 intron III sequences from GenBank and four alleles (Bmy1.a, Bmy1.b, Bmy1.c, and Bmy1.d) were identified based on indels of 126, 38, 11, and 21 bp. β-Amylase activity and thermostability were assayed in 22 North American cultivars and 12 wild barley genotypes. Cultivars carrying the Bmy1.a and Bmy1.b alleles had β-amylase activity ranges calculated on a fresh weight (FW) basis of 1.8-and 1.5-fold, respectively, and thermostability ranges of 8.8-and 1.2-fold, respectively. β-Amylase activity calculated on a protein basis yielded a 2.4-and 1.4-fold range for Bmy1.a and Bmy1.b, respectively. Significantly different activities were observed in cultivars carrying either Bmy1.a or the Bmy1.b allele when calculated on a FW basis and the Bmy1.a allele when calculated on a protein basis. Significantly different thermostabilities were observed in cultivars carrying the Bmy1.a allele. Wild barleys were found to carry Bmy1.a, Bmy1.b, and Bmy1.c alleles with β-amylase activity ranges calculated on a FW basis of 1.7-, 1.7-, and 2.6-fold, respectively, and thermostability ranges of 1.3-, 1.4-, and 2.1-fold, respectively. β-Amylase activity measured on a protein basis identified a 1.3-, 1.4-, and 2.1-fold range for Bmy1.a, Bmy1.b, and Bmy1.c, respectively. Significantly different activities were found in genotypes with any of these three alleles when calculated on a FW basis yet only in those with the Bmy1.c allele when calculated on a protein basis. Significantly different thermostabilities in genotypes carrying either the Bmy1.b or Bmy1.c allele were observed. In the germplasm studied here, the Bmy1 intron III alleles are not reliable predictors of β-amylase activity and thermostability.

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Section: Resultsmentioning

confidence: 99%

Utilization of Different Bmy1 Intron III Alleles for Predicting β-Amylase Activity and Thermostability in Wild and Cultivated Barley

2010

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“…In this study, the BAAs and BATs of Tibetan wild and cultivated barleys were compared. As a result, some wild accessions were identified which have higher BAA and BAT than those reported previously (Eglinton et al, 1998;Filichkin et al, 2010;Vinje et al, 2010). These genotypes will be useful for the improvement of malt quality through breeding programs.…”

Section: Discussionmentioning

confidence: 80%

Variation in β-amylase activity and thermostability in Tibetan annual wild and cultivated barley genotypes

Zhang

Chen

Zhang

et al. 2014

J. Zhejiang Univ. Sci. B

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β-Amylase activity (BAA) and thermostability (BAT) are important traits for malt quality. In this study, 138 Tibetan annual wild barley accessions and 20 cultivated genotypes differing in BAA were planted and analyzed in 2009 and 2012. Significant differences were detected among genotypes in BAA and BAT. The cultivated genotypes had a mean BAA of 1137.6 U/g and a range of from 602.1 to 1407.5 U/g, while the wild accessions had a mean of 1517.9 U/g and a range of from 829.7 to 2310.0 U/g. The cultivated genotypes had a mean relative residual β-amylase activity (RRBAA) of 61.6% and a range of from 22.2% to 82.3%, while the wild barleys had a mean of 57.8% and a range of from 21.9% to 96.1%. Moreover, there was a significant difference among genotypes in the response of RRBAA to the temperature and duration of heat treatment. The wild barleys had wider variation in BAA and BAT than cultivated genotypes.

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“…Morex (Clark et al 2005). In contrast, there have been numerous amino acid substitutions reported in the 'endosperm-speciWc' -amylase, encoded by Bmy1, which also has the highly polymorphic third intron (Clark et al 2003;Eglinton et al 1998;Erkkilä et al 1998;Erkkilä 1999;Erkkilä and Ahokas 2001;Filichkin et al 2010;Ma et al 2000Ma et al , 2001Sjakste and Zhuk 2006;Vinje et al 2010Vinje et al , 2011.…”

Section: Dna and Amino Sequence Analysismentioning

confidence: 99%

Differential expression of two β-amylase genes (Bmy1 and Bmy2) in developing and mature barley grain

Vinje

Willis

Duke

et al. 2011

Planta

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Two barley (Hordeum vulgare L.) β-amylase genes (Bmy1 and Bmy2) were studied during the late maturation phase of grain development in four genotypes. The Bmy1 and Bmy2 DNA and amino acid sequences are extremely similar. The largest sequence differences are in the introns, seventh exon, and 3' UTR. Accumulation of Bmy2 mRNA was examined in developing grain at 17, 19, and 21 days after anthesis (DAA). One genotype, PI 296897, had significantly higher Bmy2 RNA transcript accumulation than the other three genotypes at all developmental stages. All four genotypes had Bmy2 mRNA levels decrease from 17 to 19 DAA, and remain the same from 19 to 21 DAA. Levels of Bmy1 mRNA were twenty thousand to over one hundred thousand times more than Bmy2 mRNA levels in genotypes Legacy, Harrington, and Ashqelon at all developmental stages and PI 296897 at 19 and 21 DAA. PI 296897 had five thousand times more Bmy1 mRNA than Bmy2 mRNA at 17 DAA. However, Bmy2 protein was not found at 17 DAA in any genotype. The presence of Bmy2 was immunologically detected at 19 DAA and was present in greater amounts at 21 DAA. Also, Bmy2 protein was found to be stored in mature grain and localized in the soluble fraction. However, Bmy1 protein was far more prevalent than Bmy2 at all developmental stages in all genotypes. Thus, the vast majority of β-amylase activity in developing and mature grain can be attributed to endosperm-specific β-amylase.

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Phenotypic Variation for Diastatic Power, β‐Amylase Activity, and β‐Amylase Thermostability vs. Allelic Variation at the Bmy1 Locus in a Sample of North American Barley Germplasm

Cited by 29 publications

References 45 publications

Utilization of Different Bmy1 Intron III Alleles for Predicting β-Amylase Activity and Thermostability in Wild and Cultivated Barley

Utilization of Different Bmy1 Intron III Alleles for Predicting β-Amylase Activity and Thermostability in Wild and Cultivated Barley

Variation in β-amylase activity and thermostability in Tibetan annual wild and cultivated barley genotypes

Differential expression of two β-amylase genes (Bmy1 and Bmy2) in developing and mature barley grain

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