Purification and Properties of a Neutral Protease Produced by Lactobaccillus Brevis

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dc.contributor.authorIlori, Matthew O.
dc.contributor.authorAmund, Olukayode O.
dc.contributor.authorOmidiji, O.
dc.date.accessioned2019-06-24T13:10:42Z
dc.date.available2019-06-24T13:10:42Z
dc.date.issued1990-09-01
dc.description.abstractAn extracellular glucose-forming amylase was produced by Lactobacillus brevis isolated from ‘Kagasok tea’. The enzyme was purified 70-fold and had optimal activity at 55 oC and pH 6.5. Its Km value for starch was 0.27 mg ml-1 and its M, was approx. 75,900 Da. The activity of the enzyme was enhanced by Ca2+, Mg2+, Na+ or K+ and inhibited by EDTA, KCN, citric acid and L-cysteine.en_US
dc.identifier.citationAmund, O.O, Omidiji, O and Ilori, O (1990) Purification and Properties of a Neutral Protease Produced by Lactobaccillus Brevis. Journal of Biotechnology (13)en_US
dc.identifier.urihttps://doi.org/10.1007/BF00286381
dc.identifier.urihttp://repository.elizadeuniversity.edu.ng/handle/20.500.12398/130
dc.language.isoenen_US
dc.publisherKluwer Academic Publishersen_US
dc.subjectTempretureen_US
dc.subjectEnzymeen_US
dc.titlePurification and Properties of a Neutral Protease Produced by Lactobaccillus Brevisen_US
dc.typeArticleen_US
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