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expressão da alfa e beta amilase durante a ... - Deag.ufcg.edu.br

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72 Expressão <strong>da</strong> <strong>alfa</strong> e <strong>beta</strong> <strong>amilase</strong> <strong>durante</strong> a germinação de ceva<strong>da</strong> Santos et al.<<strong>br</strong> />

<strong>beta</strong> <strong>amilase</strong> e encerrar a germinação é<<strong>br</strong> />

fun<strong>da</strong>mental para atingir bons resultados na<<strong>br</strong> />

maltagem. Para Georg-kramer et al. (2000)<<strong>br</strong> />

muitas empresas produtoras de malte vêm<<strong>br</strong> />

tentando r<strong>edu</strong>zir o período de germinação no<<strong>br</strong> />

processo de maltagem, o que permitiriam a<<strong>br</strong> />

r<strong>edu</strong>ção de despesas e a maltagem de uma<<strong>br</strong> />

quanti<strong>da</strong>de de grãos em menos tempo. O<<strong>br</strong> />

processo de maltagem induz a germinação e<<strong>br</strong> />

assegura o crescimento <strong>da</strong> semente com<<strong>br</strong> />

produção de <strong>beta</strong> <strong>amilase</strong> de relevante<<strong>br</strong> />

influência no poder diastático.<<strong>br</strong> />

CONCLUSÃO<<strong>br</strong> />

Existe sempre uma tendência de aumento<<strong>br</strong> />

na ativi<strong>da</strong>de <strong>da</strong>s duas enzimas.<<strong>br</strong> />

A <strong>beta</strong> <strong>amilase</strong> apresenta maiores<<strong>br</strong> />

ativi<strong>da</strong>des que a <strong>alfa</strong> <strong>amilase</strong> nas condições<<strong>br</strong> />

testa<strong>da</strong>s<<strong>br</strong> />

Os maiores aumentos de ativi<strong>da</strong>de <strong>da</strong> <strong>alfa</strong><<strong>br</strong> />

<strong>amilase</strong> acontecem após 24 e 72 horas de<<strong>br</strong> />

germinação. Já para <strong>beta</strong> <strong>amilase</strong> os maiores<<strong>br</strong> />

incrementos <strong>da</strong> ativi<strong>da</strong>de específica ocorrem<<strong>br</strong> />

após 24, 32, e 64 horas de germinação.<<strong>br</strong> />

O estudo dos maiores aumentos dessa<<strong>br</strong> />

enzima em função do faixa de tempo de<<strong>br</strong> />

germinação forneceu informações necessária<<strong>br</strong> />

para produção de malte com teores enzimáticos<<strong>br</strong> />

variados, podendo ser utilizado na hidrólise de<<strong>br</strong> />

amidos de varias origens.<<strong>br</strong> />

REFERÊNCIAS BIBLIOGRÁFICAS<<strong>br</strong> />

Adewale, I. O.; Agumanu, E. N.;Otihokoronkwo,<<strong>br</strong> />

F.I. Comparative studies on<<strong>br</strong> />

#x3b1;-amylases from malted maize (Zea<<strong>br</strong> />

mays), millet (Eleusine coracana) and<<strong>br</strong> />

Sorghum (Sorghum bicolor). Carboidrate<<strong>br</strong> />

polymers, v.22, p. 2-16, 2006.<<strong>br</strong> />

Bernfeld, P. Amylase α and β in methods<<strong>br</strong> />

in enzymology. In: Colowick, S.P., Kaplan,<<strong>br</strong> />

N. (Eds.). New York: Academic Press, 1955,<<strong>br</strong> />

149p.<<strong>br</strong> />

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functional properties of the enzymes. Plant<<strong>br</strong> />

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malting. Journal of cereal science, v. 33,<<strong>br</strong> />

p.279-288, 2000.<<strong>br</strong> />

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Food Research International, v 35, p. 315–<<strong>br</strong> />

321, 2002.<<strong>br</strong> />

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Kramhøft, B.; Furniss, C. S. M.; Planchot,<<strong>br</strong> />

V.; Archer, D. B.; Williamson, G.;<<strong>br</strong> />

Svensson, B. The activity of barley α-<<strong>br</strong> />

amylase on starch granules is enhanced by<<strong>br</strong> />

fusion of a starch binding domain from<<strong>br</strong> />

Aspergillus niger glucoamylase.<<strong>br</strong> />

Biochimical et biophysica (BBA) –<<strong>br</strong> />

Proteins & Proteomics, v. 1764, p. 275–<<strong>br</strong> />

284, 2006.<<strong>br</strong> />

Kunze, W. Technology <strong>br</strong>ewing and malting.<<strong>br</strong> />

Research and teaching institute of<<strong>br</strong> />

<strong>br</strong>ewing, 1996. Disponível em: < http://<<strong>br</strong> />

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Ma, Y.; Langridge, P.; Logue, S. J.; Evans D.<<strong>br</strong> />

E. A Single Amino Acid Substitution that<<strong>br</strong> />

Determines IEF Band Pattern of Barley<<strong>br</strong> />

Beta-amylase. Journal of Cereal Science,<<strong>br</strong> />

v.35, p. 79 – 84, 2002.<<strong>br</strong> />

Macgregor, E.A.; Janecek, S.; Svensson, B.<<strong>br</strong> />

Relationship of sequence and structure to<<strong>br</strong> />

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Biochim. Biophys., Acta 1546, p. 1–20,<<strong>br</strong> />

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Maya-ampudia, V.; Bernal-lugo, I. Redoxsensitive<<strong>br</strong> />

target detection in gibberellic acidinduced<<strong>br</strong> />

barley aleurone layer. Free radical<<strong>br</strong> />

biology and medicine, v. 40, p.1362 –<<strong>br</strong> />

1368, 2006.<<strong>br</strong> />

Mohan, B.H.; Gopal, A.; Malleshi, N.G.;<<strong>br</strong> />

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and enzymatically hydrolyzed ragi (Eleusine<<strong>br</strong> />

Revista Brasileira de Produtos Agroindustriais, Campina Grande, v.12, n.1, p.67-73, 2010

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