Characterization and chillproofing activity of two enzymes from Streptomyces species
✍ Scribed by C. A. Etok; O. U. Eka
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 302 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
Two enzymes, amylase and protease of Streptomyces species were purified by a combination of ion exchange chromatography and gel filtration and characterized. The amylase had an exoaction on starch yielding maltose as a major end product and was identified as beta-amylase. The purified amylase had a molecular weight of 48,000 and was maximally active at 35 degrees C and at pH 6.0. On the other hand, protease had a molecular weight of 21,000 and was most active at pH 10.0 and at a temperature of 30 degrees C. The Km or MICHAELIS constant of amylase for maize starch was 0.333 mg/ml while that of protease for casein was 2.5 mg/ml. The feasibility of using the purified protease for various industrial application especially in the chillproofing of beer is discussed.
📜 SIMILAR VOLUMES
## Abstract Two phospholipase enzymes NN1 and NN2 were purified from the venom of __Naja nigricolis nigricolis__ Reinhardt to apparent homogeneity. NN1 was purified by a two‐step anion‐exchange chromatography on DEAE‐cellulose column while NN2 was purified by a combination of anion‐exchange chromat