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Partial purification and properties of L- alanine dehydrogenase of Aspergillus terreus [electronic resource].

By:

Al-Kadeeb, Siham A

Language: English Summary language: Arabic Description: P. 5159-5168Other title:

خواص إنزيم ل- ألانين ديهيدروجينيز لفطرة اسبرجلستيريس.‪ [Added title page title]

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Mansoura University journal of agricultural sciences, 2005 v. 30 (9) [electronic resource].

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In: Mansoura Unviersity Journal of Agricultural Sciences 2005.v.30(9)Summary: L-Alanine dehydrogenase was partially purified about 13-fold in a two-step purification from the cell free extracts of Aspergillus terreus. Maximal enzyme activity occurred at pH 8.6 for reductive amination of pyruvate, where pH 10.4 for oxidative deamination of L-alanine and at a temperature of 25 cC. The Km values for pyruvate, NH/, NAOH, L-alanine and NAD+ were 4, 175.4 0.526, 16.13 and 3.3 mM respectively. The enzyme activity was activeted by Co2+, Fe2+, Zn2+ , Ca2+, and Cu2+. SH groups don't seem to play a role in the catalytic action of the enzyme as addition of iodoacetate or dithiothreitol did not affected the enzyme activity. Stability of the enzyme under different conditions was investigated.

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L-Alanine dehydrogenase was partially purified about 13-fold in a two-step purification from the cell free extracts of Aspergillus terreus. Maximal enzyme activity occurred at pH 8.6 for reductive amination of pyruvate, where pH 10.4 for oxidative deamination of L-alanine and at a temperature of 25 cC. The Km values for pyruvate, NH/, NAOH, L-alanine and NAD+ were 4, 175.4 0.526, 16.13 and 3.3 mM respectively. The enzyme activity was activeted by Co2+, Fe2+, Zn2+ , Ca2+, and Cu2+. SH groups don't seem to play a role in the catalytic action of the enzyme as addition of iodoacetate or dithiothreitol did not affected the enzyme activity. Stability of the enzyme under different conditions was investigated.

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