Molecular Cloning and Characterizations of Xylanase Inhibitor Protein from Wheat (Triticum Aestivum).
J Food Sci
; 82(7): 1582-1587, 2017 Jul.
Article
em En
| MEDLINE
| ID: mdl-28613409
ABSTRACT
Xylanase inhibitor proteins (XIPs) were regarded to inhibit the activity of xylanases during baking and gluten-starch separation processes. To avoid the inhibition to xylanases, it is necessary to define the conditions under which the inhibition takes place. In this study, we cloned the XIP gene from 2 different variety of Triticum aestivum, that is, Zhengmai 9023 and Zhengmai 366, and investigated the properties of XIP protein expressed by Pichia pastoris. The results showed that the 2 XIP genes (xip-9023 and xip-366) were highly homologous with only 3 nucleotide differences. XIP-9023 showed the optimal inhibition pH and temperature were 7 °C and 40 °C, respectively. Inhibition of xylanase by XIP-9023 reached the maximum in 40 min. At 50% inhibition of xylanase, the molar ratio of inhibitor xylanase was 261. XIP-9023 was active to various fungal xylanases tested as well as to a bacterial xylanase produced by Paenibacillus sp. isolated from cow rumen.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
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Triticum
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Clonagem Molecular
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Endo-1,4-beta-Xilanases
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Inibidores Enzimáticos
Limite:
Animals
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article