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linamarase/manihot esculenta

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The cyanogenic beta-glucosidase (linamarase) of cassava is responsible for the first step in the sequential break-down of two related cyanoglucosides. Hydrolysis of these cyanoglucosides occurs following tissue damage and leads to the production of hydrocyanic acid. This mechanism is widely regarded

Cassava latex as a source of linamarase for determination of linamarin.

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A major constraint in the enzymatic assays for determination of linamarin in cassava is the preparation of purified linamarase. Cassava latex, which exhibits high linamarase activity, was tried as an alternate source of the enzyme. Enzyme yield from latex was compared with that from rind and leaf.

Changes of cyanide content and linamarase activity in wounded cassava roots.

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When cassava (Manihot esculenta Crantz) root was cut into blocks and incubated under laboratory conditions, the blocks showed more widespread and more even symptoms of physiological deterioration than those under natural conditions. Thus, the tissue block system has potential for biochemical studies

Linamarase expression in cassava cultivars with roots of low- and high-cyanide content.

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This paper reports the expression and localization of linamarase in roots of two cassava (Manihot esculenta Crantz) cultivars of low and high cyanide. Two different patterns of linamarase activity were observed. In the low-cyanide type, young leaves displayed very high enzyme activity during the

Characterization of cyanogenic beta-glucosidase (linamarase) from cassava (Manihot esculenta Crantz).

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Linamarase (EC 3.2.1.21) was purified from cassava petiole, stem, and root cortex by ammonium sulfate precipitation, column chromatography on Sepharose 6B, and chromatofocusing. The last step resolved the enzyme from each source into three forms with pI values of 4.3, 3.3, and 2.9. Each form was

Immobilization of linamarase and its use in the determination of bound cyanide in cassava using flow injection analysis.

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Extracts from the tubers (cortex and parenchyma) and leaves of Manihot esculenta Crantz (cassava) were analyzed for their releasable cyanide content using flow injection analysis incorporating an immobilized linamarase bioreactor. Linamarase was immobilized under very mild conditions to an activated

Characterization of linamarase of latex and its localization in petioles in cassava.

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The distribution of linamarase in latex and its purification, characterization, and immunocytochemical localization in petioles were studied in order to get an insight into the process of cyanogenesis in cassava. Crude latex exudate exhibited low linamarase activity, but on dilution the activity
The coding sequence of the mature cyanogenic beta-glucosidase (beta-glucoside glucohydrolase, EC 3.2.1.21; linamarase) was cloned into the vector pYX243 modified to contain the SUC2 yeast secretion signal sequence and expressed in Saccharomyces cerevisiae. The recombinant enzyme is active,

Purification, characterization, and localization of linamarase in cassava.

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We have purified cassava (Manihot esculenta) linamarase to apparent homogeneity using a simplified extraction procedure using low pH phosphate buffer. Three isozymes of cassava linamarase were identified in leaves based on differences in isoelectric point. The enzyme is capable of hydrolyzing a
The broad-specificity cyanogenic beta-D-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) (linamarase) from Manihot esculenta Crantz (cassava) was irreversibly inactivated by N-bromoacetyl-beta-D-glucopyranosylamine according to pseudo-first-order kinetics with a second-order efficiency
The broad-specificity cyanogenic beta-D-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) (linamarase) from Manihot esculenta Crantz (cassava) was kinetically characterized in mixed substrate systems and with the transition-state analogue glucono(1-5)lactone and a series of 1-thio substrate

Linamarin sensors:  interference-based sensing of linamarin using linamarase and peroxidase.

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An interference-based linamarin sensor is developed. Horseradish peroxidase (HRP) is adsorbed on a pyrolytic graphite (PG) electrode, and then linamarase from cassava is cross-linked with glutaraldehyde on the electrode surface. The prepared bienzyme electrode is poised at -300 mV vs Ag/AgCl for 40

Cyanide detoxification in cassava for food and feed uses.

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Cassava (Manihot esculenta Crantz) is an important tropical root crop providing energy to about 500 million people. The presence of the two cyanogenic glycosides, linamarin and lotaustralin, in cassava is a major factor limiting its use as food or feed. Traditional processing techniques practiced in

Assessing cyanogen content in cassava-based food using the enzyme-dipstick method.

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The cyanogen content of 35 cassava-based foods was determined using the enzyme-dipstick method. The analyses showed presence of residual cyanogens in these products, and they ranged from 2 to 88 mg HCN equivalent/kg. Foodstuff prepared from grated cassava roots exhibited a lower level of cyanogen

The contribution of moulds and yeasts to the fermentation of 'agbelima' cassava dough.

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Agbelima, a fermented cassava meal widely consumed in Ghana, Togo and Benin, is produced by fermenting grated cassava with one of several types of traditional cassava dough inoculum. During fermentation a smooth textured sour dough is produced, the toxicity of cassava is reduced and there is a build
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