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The pH and thermal response of purified leucine-specific aminopeptidase from aeromonas caviae

A purified extracellular monomeric leucine-specifìc aminopeptidase from Aeromonas caviae T-58 with molecular mass of 32 kDa was subjected to varying pH and temperature conditions to determine its response. The activity of the enzyme was maximal at 65°C but stable up to 40°C. Optimum pH was 8.0 and p...

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Format: Conference Proceeding
Published: 2008-09
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LEADER 00000njm a2000000a 4500
001 oai:repository.ui.edu.ng:123456789/4769
042 |a dc 
720 |a Abu, O. A.  |e author 
720 |a Hayashi, K.  |e author 
260 |c 2008-09 
520 |a A purified extracellular monomeric leucine-specifìc aminopeptidase from Aeromonas caviae T-58 with molecular mass of 32 kDa was subjected to varying pH and temperature conditions to determine its response. The activity of the enzyme was maximal at 65°C but stable up to 40°C. Optimum pH was 8.0 and pH stability had a range of 6 and 10. 
024 8 |a 978-3477-2-2 
024 8 |a In: Bawa, G. S., Akpa, G. N., Jokthan. G. E.. Kabir M. and Abdu S. B. (Eds.) Proceedings of 13th Annual Conference of the Animal Science Association of Nigeria, on Repositioning Animal Agriculture for the realization of National Vision 2020, held at Ahmadu Bello University, Zaria, Nigeria between September 15th-19th 2008, pp. 118-120 
024 8 |a ui_inpro_abu_pH_2008 
024 8 |a http://ir.library.ui.edu.ng/handle/123456789/4769 
245 0 0 |a The pH and thermal response of purified leucine-specific aminopeptidase from aeromonas caviae