Abstract：
:A serine alkaline protease from a newly isolated alkaliphilic Bacillus altitudinis GVC11 was purified and characterized. The enzyme was purified to homogeneity by acetone precipitation, DEAE-cellulose anion exchange chromatography with 7.03-fold increase in specific activity and 15.25% recovery. The molecular weight of alkaline protease was estimated to be 28 kDa by SDS PAGE and activity was further assessed by zymogram analysis. The enzyme was highly active over a wide range of pH 8.5 to 12.5 with an optimum pH of 9.5. The optimum temperature of purified enzyme was 45 °C and Ca(2+) further increased the thermal stability of the enzyme. The enzyme activity was enhanced by Ca(2+) and Mg(2+) and inhibited by Hg(2+). The present study is the first report to examine and describe production of highly alkaline protease from Bacillus altitudinis and also its remarkable dehairing ability of goat hide in 18 h without disturbing the collagen and hair integrity.
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Vijay Kumar E,Srijana M,Kiran Kumar K,Harikrishna N,Reddy Gdoi
10.1007/s00449-010-0483-xsubject
Has Abstractpub_date
2011-05-01 00:00:00pages
403-9issue
4eissn
1615-7591issn
1615-7605journal_volume
34pub_type
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