@article{oai:ir.kagoshima-u.ac.jp:00010746,
 author = {SAKATA, Taizo and SUMIYOSHI, Kazuro and KAKIMOTO, Daiichi},
 journal = {鹿児島大学水産学部紀要=Memoirs of Faculty of Fisheries Kagoshima University},
 month = {2016-10-31},
 note = {Four components with casein hydrolysing activity were found in extracellular protease produced by a marine Pseudomonas sp. I-6. Each protease component was fractionated by use
of DEAE-Sephadex A-50, Sephadex G-100 and polyacrylamide gel electrophoresis. Protease
activity was determined by the digestion of casein in the reaction mixture for fractions obtained
on column chromatography and on a casein agar plate for polyacrylamide gels, respectively.
The method of a casein agar plate was found to be convenient to detect the protease activity
on the gel.
Protease fractions were alkaline proteases of which optimal pHs were from pH 10.0 to pH
11.0. Proteases F-IIa and F-IIb were very low in activity without Ca^++ ion but reactivated
with the addition of Ca^++ ion remarkably, whereas the activities of F-Ia and F-Ib were unaffected or slightly affected by Ca^++ ion. Proteases of this strain were stabilized to heat by
Ca^++ ion but no substantial decrease in activity was observed during 6 hr incubation at 25 C
regardless of the absence of Ca^++ ion.},
 pages = {71--78},
 title = {Studies on the Proteases of Marine Bacteria III : Purification and Some Enzymatic Properties of Proteases},
 volume = {26},
 year = {}
}