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

dc.contributor.authorAbu, O. A.
dc.contributor.authorHayashi, K.
dc.date.accessioned2019-09-19T14:42:05Z
dc.date.available2019-09-19T14:42:05Z
dc.date.issued2008-09
dc.description.abstractA 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.en_US
dc.identifier.issn978-3477-2-2
dc.identifier.otherIn: 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
dc.identifier.otherui_inpro_abu_pH_2008
dc.identifier.urihttp://ir.library.ui.edu.ng/handle/123456789/4769
dc.language.isoenen_US
dc.publisherAnimal Science Association of Nigeriaen_US
dc.titleThe pH and thermal response of purified leucine-specific aminopeptidase from aeromonas caviaeen_US
dc.typeOtheren_US

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