scholarly journals The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27

1967 ◽  
Vol 104 (3) ◽  
pp. 953-959 ◽  
Author(s):  
C Anthony ◽  
LJ Zatman
1969 ◽  
Vol 130 ◽  
pp. 422-429 ◽  
Author(s):  
Katsuko Suhara ◽  
Shigeki Takemori ◽  
Masayuki Katagiri

1974 ◽  
Vol 38 (10) ◽  
pp. 1819-1833 ◽  
Author(s):  
Akikazu Hatanaka ◽  
Tadahiko Kajiwara ◽  
Susumu Tomohiro

1980 ◽  
Vol 26 (7) ◽  
pp. 833-838 ◽  
Author(s):  
Hiromi Kobori ◽  
Nobuo Taga

Extracellular alkaline phosphatase produced by a marine Pseudomonas was purified to electrophoretic homogeneity. The molecular weight of the enzyme was estimated to be 100 000. The enzyme had maximal activity at pH 11.5. The enzyme was completely inhibited by 1 mM EDTA. However, divalent cations reversed the enzyme inhibition and their order of effectiveness on the reaction was Zn2+ > Ca2+ > Mn2+ > Mg2+ > Sr2+ > Co2+. The enzyme activity was affected by the species of anion whose order of effectiveness was demonstrated to follow the lyotrophic series, Cl− > Br− > NO3−> ClO4− > SCN−. The activity of phosphatase was accelerated linearly by increased pressure until up to 1000 atm (1 atm = 101.325 kPa), and the enzyme activity at 1000 atm was 3.2 times higher than that at 1 atm.


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