1996
DOI: 10.1002/(sici)1097-0010(199604)70:4<509::aid-jsfa532>3.0.co;2-7
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Purification and Some Properties of Glutaminase fromActinomucor taiwanensis,Starter of Sufu

Abstract: Glutaminase of Actinomucor taiwanensiswas purified approximately 96‐fold with a yield of 18%, by sequential fractionation with ammonium sul‐phate, anion exchange with DEAE‐Sepharose CL‐6B and gel filtration with Sephacryl S‐200. The pH and temperature optima of purified glutaminase were 8·0 and 45°C, respectively. Glutaminase was stable at a temperature up to 35°C and at pH values of 6·0–8·0. The molecular weight was 80000 as determined from SDS‐PAGE. The enzyme activity was markedly inhibited by HgCl2. In the… Show more

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Cited by 15 publications
(9 citation statements)
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“…The activity decreased when CuSO 4 , ZnSO 4 and EDTA were used. These results are in accordance to glutaminase from Actinomucor taiwanensis reported by Lu et al (1996) who indicated that the activity of glutaminase from Actinomucor taiwanensis was enhanced by the addition of MgSO 4 and NaCl. It was also highly stable in the presence of sodium hypochlorite and hydrogen peroxide at 30°C and pH 7 with activity (21.7 and 21.4 U/ml) respectively (Table 4).…”
Section: Properties Of the Partially Purified Enzymesupporting
confidence: 92%
“…The activity decreased when CuSO 4 , ZnSO 4 and EDTA were used. These results are in accordance to glutaminase from Actinomucor taiwanensis reported by Lu et al (1996) who indicated that the activity of glutaminase from Actinomucor taiwanensis was enhanced by the addition of MgSO 4 and NaCl. It was also highly stable in the presence of sodium hypochlorite and hydrogen peroxide at 30°C and pH 7 with activity (21.7 and 21.4 U/ml) respectively (Table 4).…”
Section: Properties Of the Partially Purified Enzymesupporting
confidence: 92%
“…hydrolysis of glutamine to glutamate from A. tai-Ž . wanensis were studied by Lu et al 1996 . Glutaminase was stable at a temperature up to 358C and at pH values of 6.0-8.0.…”
mentioning
confidence: 99%
“…Glutaminases from various species of organisms behave differently in the presence of NaCl. Glutaminase I of Micrococcus luteus K-3 was activated by about 30% in the presence of 16% w/v NaCl [22], whereas glutaminase II was not [23]. Glutaminase of Actinomucor taiwanensis exhibited inactivation to some extent in the presence of NaCl [22].…”
Section: Effect Of Naclmentioning
confidence: 99%
“…Glutaminase I of Micrococcus luteus K-3 was activated by about 30% in the presence of 16% w/v NaCl [22], whereas glutaminase II was not [23]. Glutaminase of Actinomucor taiwanensis exhibited inactivation to some extent in the presence of NaCl [22]. Glutaminases from Escherichia coli, Pseudomonas fluorescens, Cryptococcus albidus, Aspergillus oryzae, and Aspergillus sojae showed 65%, 75%, 65%, 20%, and 6% residual activity, respectively, in 18% w/v NaCl [24].…”
Section: Effect Of Naclmentioning
confidence: 99%