Studies on the hydrolysis of lecithin by a Penicillium notatum phospholipase B preparation.
نویسنده
چکیده
منابع مشابه
Reminiscence of phospholipase B in Penicillium notatum
Since the phospholipase B (PLB) was reported as a deacylase of both lecithin and lysolecithin yielding fatty acids and glycerophosphocholine (GPC), there was a question as to whether it is a single enzyme or a mixture of a phospholipase A2 (PLA2) and a lysophospholipase (LPL). We purified the PLB in Penicillium notatum and showed that it catalyzed deacylation of sn-1 and sn-2 fatty acids of 1,2...
متن کاملSTUDIES ON PHOSPHOLIPASE C FROM MELIA AZADIRACHTA SEEDS
The activity of phospholipase C in crude enzymatic preparation of Melia azadiracht seeds (Neem seeds) was studied by the use of lecithin as a substrate in aqueous medium. The enzyme activity was found optimum at pH 2.5 and temperature 35?C. The phospholipase C was found heat labile, being inactivated 88% within 10 minutes at 90°C
متن کاملThe activation of surface films of lecithin by amphipathic molecules.
In the preceding paper it was shown that a phospholipase prepared,from Penicllium notatum will hydrolyse lecithin only after the, addition,, of a minimum proportion of anionic amphipathic molecules1 e.g. dicetylphosphoric acid, cardiolipin, sodium dodecyl sulphate (Bangham & Dawson, 1959), The onset of hydrolysis occurred, only when the emulsion particles carried a minimum net negative charge, ...
متن کاملPurification of phospholipase B from Penicillium notatum by hydrophobic chromatography on palmitoyl cellulose.
Phospholipase B (lysolecithin acyl-hydrolase, EC 3.1.1.5) from the mycelia of Penicillium notatum (Institute for Fermentation, Osaka, Japan; No.4640) was adsorbed from a crude solution to palmitoyl cellulose. Adsorption was efficient at pH 4 at low ionic strength (10 mM buffer), and at pH 4-9 at higher ionic strength (1-2M NaCl in 10 mM buffer). The adsorbed enzyme was eluted from the cellulose...
متن کاملErrata to “Reminiscence of phospholipase B in Penicillium notatum”
In this paper, following corrections should be made: (page 336, Fig. 4) Replace the figure as follows: (page 336, legend of Fig. 4, line 2) For " S-125 " Read " S-128 " (continues to the next page)
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 70 4 شماره
صفحات -
تاریخ انتشار 1958