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Ray, R. R., Nanda, G.: β-amylases biosynthesis, characteristics and industrial applications. Critical Rev in Microbiol 22 , 181-199 (1996). β-amylases biosynthesis, characteristics and

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–619. McCleary, B.V. and Codd, R. (1989). Measurement of β-amylase in cereal flours and commercial enzyme preparations. Journal of Cereal Science 9: 17–33. Codd R. Measurement of β-amylase

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75 82 Evans, D.E., Wallace, W., Lance, R.C.M., Eglington J.K., Logue, S.J., Barr, A.R. 1995. The influence of β -amylase isoform pattern on β -amylase activity on barley and malt

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. (Coeliac disease — Emerging public health issue of the XXI st century). www.mimnet.hu Okungbowa, J., Obeta, J.A.N. & Ezeogu, L.I. (2002): Sorghum β-amylase production: relationship with grain cultivar

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Paeonia decomposita is a perennial deciduous shrub with great ornamental and medicinal values. Unfortunately, the distribution region, population size and individual numbers of P. decomposita rapidly decrease in the wild. It is a particularly rare, highly endangered, protective plant endemic to Southwest China. To understand the causes of seed dormancy of P. decomposita, the effects of aqueous extracts of the seed coat, endosperm of P. decomposita on germination, seedling growth and amylases activities of wheat seeds were examined in this paper. The results showed that the seed, especially the endosperm tissue of P. decomposita contained substances that strongly suppressed seed germination. The crude extract of endosperm of P. decomposita, which significantly reduced the activities of α and β-amylase, showed a more significant inhibition than that of seed coat at the same dose. It was concluded that the presence of inhibitory substances in seed, especially in endosperm tissue, seem to be responsible for P. decomposita seed dormancy.

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Currently gluten-free beer is not produced in Hungary for coeliacs. The goal of our research was to develop brewery products made of domestically grown millet (Alföldi 1) and buckwheat (Oberon) that are similar to traditional beer of barley malt regarding taste, aroma, consistency, colour, foam stability and alcohol content.On a micromalting equipment malts were made of buckwheat and millet. Beer was produced on pilot plant scale (50 l) with decoction process (mashing program with rests at 50 °C, 65 °C and 72 °C) and was supplemented with a highly heat-stable bacterial α-amylase, a fungal α-amylase and β-glucanase. Malts were evaluated by congress mashing (extract content, extract difference, pH, and colour); wort and final beer analyses were performed as well (pH, extract, iodine test, FAN, colour, bitterness, alcohol and extract content). Finally, sensory characterization was carried out. Difficulties with lautering were encountered during the brewing process with buckwheat. The analytical results indicated that the buckwheat and millet beer had different values compared with a typical barley beer with regard to pH, FAN, fermentability, and total alcohol. The extracts of the buckwheat and millet wort were lower, resulting in a final attenuation of 61.5% and 73.2%.In laboratory experiments optimal temperature of β-amylase found in domestically grown buckwheat (64 °C) and millet (62 °C) was determined by detecting maltose production with HPLC. Data was used to set the rest temperature of the enzyme during mashing. Inhibiting effect of certain substances on proteolytic enzymes was investigated by measuring the extract, FAN, and soluble nitrogen contents. Inhibition was detected in case of both raw materials, although to a different extent. Inhibition is influenced by tannins and polyphenols found in the grain (Chethan et al., 2008).

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. Evans, E., van Wegen, B., Ma, Y.F., Eglinton, J. 2003. The impact of the thermostability of α -amylase, β -amylase, and limit dextrinase on potential wort fermentability. J. Am. Soc. Brew. Chem. 61 :210

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1466 1469 Sharp, P.G., Kreis, M., Shewry, P.R., Gale, M.D. 1988. Location of β -amylase sequence in wheat and its relatives. Theor. Appl. Genet. 75 :289

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P.R., Gale M.D. (1988): Location of β-amylase sequence in wheat and its relatives. Theor. Appl. Genet. 75:289–290. Gale M.D. Location of β-amylase sequence in wheat and its

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Sharp, P.J., Kreis, M., Shewry, P. 1988. Location of β-amylase sequences in wheat and its relatives. Theor. Appl. Genet. 75 :289–290. Shewry P. Location of β-amylase sequences in

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