Cleavage of bacillus subtilis endo-β-1,4-glucanase by B. megaterium protease

✍ Scribed by Dong Ho Ahn; Hoon Kim; M. Y. Pack

• Book ID: 104634822
• Publisher: Springer Netherlands
• Year: 1993
• Tongue: English
• Weight: 370 KB
• Volume: 15
• Category: Article
• ISSN: 0141-5492
• DOI: 10.1007/bf00133011

✦ Synopsis

A protease secreted by B. megaterium ATCC 14945 was purified by ammonium sulfate fractionation, Q-Sepharose, Sephadex G-75, and hydroxyapatite chromatography and its molecular weight was estimated to be 38 kD. The purified protease caused the cleavage of 52 kD B. subtilis endo+1,4-glucanase expressed in B. megaterium. The enzyme was most active at pH 7.5 and 55 "C. Calcium ion was required for the enzyme activity and the activity was almost completely inhibited by EDTA. The protease was not inhibited by phenylmethylsulfonyl fluoride.