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Journal ArticleDOI

Release and activation of barley Beta-amylase by malt endopeptidases

J. R. Guerin, +2 more
- 01 Jan 1992 - 
- Vol. 15, Iss: 1, pp 5-14
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TLDR
The activity of free beta-amylase, extracted from quiescent barley seed, was also increased by treatment with 2-ME and the endopeptidases, and two isoforms found in germinated barley were not present in the endopesptidase-treated samples, however.
About
This article is published in Journal of Cereal Science.The article was published on 1992-01-01. It has received 56 citations till now. The article focuses on the topics: Hordeum vulgare & Amylase.

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Citations
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Journal ArticleDOI

Molecular basis of barley quality

TL;DR: Genomic techniques allowing more detailed analysis of variations in the barley genome in relation to quality promise to extend significantly the value of molecular genetic approaches to barley quality improvement.
Journal ArticleDOI

Thermostability variation in alleles of barley beta-amylase

TL;DR: Thermostability assays in conjunction with IEF and molecular mapping were used to identify three beta-amylase alleles in cultivated barley and an additional allele in an accession of wild barley, suggesting that increased thermostability results in more efficient starch degradation.
Book ChapterDOI

Gibberellin Action in Germinated Cereal Grains

TL;DR: In this article, the response of cereal aleurone to gibberellin and abscisic acid (GA and ABA), particularly with reference to a-amylase synthesis, has made a significant contribution to our understanding of GA action in plant cells.
Journal ArticleDOI

Genetic and environmental variation in the diastatic power of australian barley

TL;DR: The results indicate the need to select barley cultivars separately for alpha-amylase and beta-amymylase activities to achieve high levels of diastatic power.
Journal ArticleDOI

Allele-Dependent Barley Grain β-Amylase Activity

TL;DR: It is demonstrated that the high β-amylase trait in the backcross line is co-inherited with the β-amy1 gene from the H. spontaneum parent, and the involvement of specific intron III sequences, in particular a 126-bp palindromic insertion, in the allele-dependent expression of β-AMylase activity in barley grain is proposed.
References
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Journal ArticleDOI

Measurement of cereal α-amylase: A new assay procedure

TL;DR: A new procedure for the assay of cereal α-amylase has been developed, which shows an excellent correlation with the Farrand, the Falling Number and the Phadebas α- amylase assay procedures.
Journal ArticleDOI

Primary structure and differential expression of β-amylase in normal and mutant barleys

TL;DR: Southern blotting of genomic DNA demonstrates that beta-amylase is encoded by a small gene family, while cDNA sequence analysis indicates the presence of at least two types of mRNA in the endosperm.
Journal ArticleDOI

Release and Activity of Bound β-Amylase in a Germinating Barley Grain

TL;DR: In resting grains of Triumph barley, at least the bulk of the bound β-amylase is released by the proteolytic action of one or several SH-proteinases, and it is likely that the slower rate of hydrolysis is due to steric hindrances which prevent substrates from reaching the active site.
Journal ArticleDOI

A major gibberellic Acid-induced barley aleurone cysteine proteinase which digests hordein : purification and characterization.

TL;DR: The analysis of hemoglobin digestion products by both gradient SDS-PAGE and Bio-Gel P2 chromatography, the inhibition of protease activity by E-64, leupeptin, iodoacetate, and p-hydroxymercuribenzoates, and N-terminal amino acid sequence analysis all indicate that EP-B is a cysteine proteinase.
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