![An extracellular-Pepstatin insensitive acid protease produced by Thermoplasma volcanium [An article from: Bioresource Technology]](https://www.ebooknetworking.net/books/B00/0P6/bigB000P6OYQA.jpg)
An extracellular-Pepstatin insensitive acid protease produced by Thermoplasma volcanium [An article from: Bioresource Technology]
Book Details
Author(s)S. Kocabiyik, H. Ozel
PublisherElsevier
ISBN / ASINB000P6OYQA
ISBN-13978B000P6OYQ6
MarketplaceFrance 🇫🇷
Description
This digital document is a journal article from Bioresource Technology, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description:
In this study, some parameters for the production and caseinolytic activity of an extracellular thermostable acid protease from a thermoacidophilic archaeon Thermoplasma volcanium were determined. The highest level of growth and enzyme production were detected at pH 3.0 over an incubation period of 192h at 60^oC. The pH optimum for the acid protease activity was 3.0 and the enzyme was fairly stable over a broad pH range (pH 3.0-8.0). The temperature for maximum activity of the enzyme was 55^oC and activity remained stable between 50^oC and 70^oC. These features could be of relevance for various biotechnological applications of this enzyme. Serine-(PMSF), cysteine-(DTT), metallo-(EDTA) and aspartate-(pepstatin) protease inhibitors did not inhibit the caseinolytic activity of the enzyme. Therefore, Tp. volcanium acid protease could be a member of the pepstatin-insensitive carboxyl proteinases.
Description:
In this study, some parameters for the production and caseinolytic activity of an extracellular thermostable acid protease from a thermoacidophilic archaeon Thermoplasma volcanium were determined. The highest level of growth and enzyme production were detected at pH 3.0 over an incubation period of 192h at 60^oC. The pH optimum for the acid protease activity was 3.0 and the enzyme was fairly stable over a broad pH range (pH 3.0-8.0). The temperature for maximum activity of the enzyme was 55^oC and activity remained stable between 50^oC and 70^oC. These features could be of relevance for various biotechnological applications of this enzyme. Serine-(PMSF), cysteine-(DTT), metallo-(EDTA) and aspartate-(pepstatin) protease inhibitors did not inhibit the caseinolytic activity of the enzyme. Therefore, Tp. volcanium acid protease could be a member of the pepstatin-insensitive carboxyl proteinases.
