Purification and Characterization of Twoα-Amylases fromToxoplasma gondii

Ferrer, Alain; Hoebeke, Johan; Bout, Daniel

doi:10.1006/expr.1999.4404

Cited by 5 publications

(4 citation statements)

References 24 publications

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“…For example, the amylase from Prostephanus truncates was unstable when the temperature was over 40°C (Olaya, Jimênez, Rodríguez, Frier, & Labra, 2000), the amylase activity of Ruditapes variegates was stable between 4 and 35°C, but its activity was sharply lost when the temperature was higher than 40°C (Hsu, 2003). The relative a-amylase activity of tilapia was reduced to 20% when the temperature was over 50-60°C and the relative a-amylase activity of Toxoplasma gondii was <20% when the temperature was over 64°C (Ferre, Hoebeke, & Bout, 1999). In comparison to the above results, the amylase from soybean is more stable at higher temperature than the animal amylase.…”

Section: Discussionmentioning

confidence: 72%

Purification of soybean amylase by superparamagnetic particles

Lin

Kuo

et al. 2009

Food Chemistry

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Section: Discussionmentioning

confidence: 72%

Purification of soybean amylase by superparamagnetic particles

Lin

Kuo

et al. 2009

Food Chemistry

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“…1). In the case of the parasitic protozoon T. gondii, the membrane-bound a-amylase was present along with the cytoplasmic enzyme (Ferrer et al, 1999). The activity of A. suum enzyme in the cytosolic fraction of cells both from muscle and intestine was generally low; in neither case did it exceed 10% of total enzyme activity (Fig.…”

Section: Discussionmentioning

confidence: 96%

“…fering more or less in their physical, chemical and immunological properties can be simultaneously present (Strumeyer et al, 1988;Anindyawati et al, 1998;Fereyroux et al, 1998;Ferrer et al, 1999;Matsuo et al, 1999). Similarly, in A. suum at least three a-amylases differing in their properties -pseudocoelomic ( enka & Prokopiè, 1984), muscle and intestinal -were found.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of alpha-amylases from the intestine and muscle of ascaris suum (Nematoda).

Zoltowska¹

2001

Acta Biochim Pol

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Alpha-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of a-amylase from muscles with pl of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. Alpha-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal alpha-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70 degrees C and 50 degrees C, respectively. The Km values were: for muscle amylase 0.22 microg/ml glycogen and 3.33 microg/ml starch, and for intestine amylase 1.77 microg/ml glycogen and 0.48 microg/ml starch. Both amylases were activated by Ca2+ and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of a-amylase from wheat. No significant differences were found between the properties of a-amylases from parasites and from their hosts.

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“…Most of the purification protocols reported for ␣-amylases from thermophilic sources and from mesophiles are multistep processes (15,16). Lately, however, the trend has been to cut down production costs in downstream processing by introducing affinity interactions right at the beginning of the purification protocol.…”

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confidence: 99%