2012
DOI: 10.2478/s11756-012-0067-0
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Thermostable alkaline protease from newly isolated Vibrio sp.: extraction, purification and characterisation

Abstract: AbstractAn extracellular alkaline protease-producing Vibrio sp. was isolated from mangrove sediments of Vellar estuary. A 9.36-fold purification was achieved by a three-step purification procedure and the molecular weight of the enzyme was determined as 33 kDa by SDS-PAGE. The enzyme was active in a broad range of pH (6.0–11.0) and temperature (30–70°C), the optimum being at pH 9.0 and temperature 55°C. The enzyme was stable at alkaline pH range of 9–11 and up to a temperature … Show more

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Cited by 8 publications
(1 citation statement)
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“…Usually, the optimum catalysis pH for alkaline proteases (APases) ranges from 8.0 to 10.0. [34][35][36] The protease showed activity over a wide range of pH values for casein substrate hydrolysis and exhibited maximum activity at pH 10.0 (Fig. 4(A)).…”
Section: Effect Of Ph Temperature and Salinity On Protease Activitymentioning
confidence: 99%
“…Usually, the optimum catalysis pH for alkaline proteases (APases) ranges from 8.0 to 10.0. [34][35][36] The protease showed activity over a wide range of pH values for casein substrate hydrolysis and exhibited maximum activity at pH 10.0 (Fig. 4(A)).…”
Section: Effect Of Ph Temperature and Salinity On Protease Activitymentioning
confidence: 99%