Summary
An extracellular, low molecular weight alkaline proteinase (alkaline proteinase “B”) has been purified to homogeneity from the culture filtrate ofConidiobolus coronatus (NCIM 1238). A 12-fold purification was achieved with a specific activity of 29,760 u/mg. The enzyme had an optimum pH and temperature of 9.7 and 45°C respectively. It was most active towards casein and had a molecular weight of 6,800, the lowest reported so far. It was stable between pH 6.5–7.5. Alkaline proteinase “B” is a serine proteinase. It showed an esterolytic activity on N-benzoyl-L-tyrosine ethyl ester (BTEE) and was successfully used to resolve the racemic mixture of D, L-phenylalanine and D,L-phenylglycine and can thus potentially replace subtilisin Carlsberg in resolving the racemic mixture of amino acids.
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Sutar, I.I., Srinivasan, M.C. & Vartak, H.G. A low molecular weight alkaline proteinase fromConidiobolus coronatus . Biotechnol Lett 13, 119–124 (1991). https://doi.org/10.1007/BF01030462
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DOI: https://doi.org/10.1007/BF01030462