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Autore principale: Ogbonnaya Nwokoro
Natura: Artículo científico
Lingua:en
Pubblicazione: Sociedad Química de México 2011
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Accesso online:https://www.redalyc.org/articulo.oa?id=47521272010
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  • Linamarase Enzyme from Lactobacillus delbrueckii NRRL B-763: Purification and Some Properties of a B-Glucosidase Ogbonnaya Nwokoro Florence Onyebuchi Anya Multidisciplinaria (Ciencias Naturales y Exactas) cassava Linamarase enzyme cyanide detoxification Lactobacillus delbrueckii Some biochemical properties and purification of linamarase enzyme from Lactobacillus delbrueckii NRRL B-763 were studied. The crude enzyme was used to detoxify cassava flour cyanide and samples of 150 m particle size treated with the crude enzyme showed a reduction from 2.1 mg HCN/10g sample to 0.11 mg HCN/10 g sample after 20 h (95% reduction). Untreated control samples of 0.5 mm particle size showed a reduction from 2.1mg HCN/10 g sample to 1.98 mg HCN/10 g sample after 40 h (5.7% reduction). The enzyme was purified 33 fold with a 40% yield through a series of four steps namely, ammonium sulphate precipitation, acetone precipitation, ion exchange chromatography and gel filteration chromatograrphy using Sephadex G-200. The purified enzyme showed maximum activity at pH 4.5. The enzyme showed 100% stability at the pH range of 5.0 and 6.0. Maximum activity of the enzyme was observed at a temperature of 50 oC and maximum stability at a temperature range of 40 and 50 oC. The approximate enzyme molecular weight was estimated to be 56 kDa by Sephadex G-200 gel filteration chromatography. The linamarase enzyme could be adapted for improved degradation of cassava cyanide and other biotechnological applications. 2011 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47521272010 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.4 Vol.55