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E L Ruban

Publications and source records attributed to E L Ruban.

51 records · Page 3Linked to original sources
PubMedDate not supplied

[Lipolytic activity of microorganisms isolated from different sources].

From different natural sources (samples of raw and pasteurized milk, fresh and melted butter, cheese, industrial and nonindustrial sewage containing fats and surface active substances) 650 microorganisms were isolated. Measurements of their lipolytic activity on milk fat (20% cream), tristearin and olive oil indicated that 27 microorganisms had no lipolytic activity on either substrate. A hundred cultures showed the highest activity. Out of them 40 most active cultures belonging to different systematic groups (fungi, yeast, bacteria) were identified as representatives of certain genera or species. Lipolytic activity varied significantly in microorganisms belonging to the same species. The use of several substrates (cream, tristearin, olive oil) helped to discriminate microorganisms that preferentially hydrolyzed either substrate.

Animals↗
PubMedDate not supplied

[Synthesis and hydrolysis lipids in microorganisms (a review)].

The review presents current concepts of the synthesis and hydrolysis of phospholipids and triglycerides of microorganisms. The paper discusses differences in the synthesis of phospholipids in micro- and macroorganisms as well as properties an reversal of action of lipases (triglyceride hydrolases) in microorganisms.

Bacteria↗
PubMedDate not supplied

[Isolation and characterization of lipase from Geotrichum asteroides FKM F-144].

By gel chromatography on Sephadex G-75 it has been demonstrated that the culture fluid of Geotrichum asteroides VKM F-144 contains two lipolytic components, one of which, lipase 1, eluates in the free volume of the column, whereas the second component, lipase 2, eluates in the volume close to that of the egg albumin yield. The paper describes a method for lipase 2 preparation consisting of precipitation of accompanying compounds at pH 4.2, depigmentation of the supernatant on the resin PAP in the Cl-form, selective sorption of lipase on the cation exchange resin CMC and further purification of the eluate gel chromatography and Sephadex G-100 rechromatography. The molecular weight of the lipase is estimated to be 45,000 and the isoelectric point to correspond to pH 4.3. pH optimum of action of the purified enzyme, areas of its pH- and thermostability have been determined.

Geotrichum↗
PubMedDate not supplied

[Localization of the extracellular lipase in Candida paralipolytica yeasts].

The localization of lipase in the cells of Candida paralipolytica was studied for the first time by the techniques of electron cytochemistry and immunocytochemistry. Lipase is formed at the outer surface of the cytoplasmic membrane and often is confined to its invaginations. The reaction products were detected in individual parts of the periplasmic space, in the cell wall, and in its exofibrillar components. Apparently, lipase is formed on the ribosomal-membrane complex. The above pattern is observed only in the cells with a high lipase activity, but not in the control. The two techniques gave similar results. A series of electronograms are presented.

Animals↗
PubMedDate not supplied

[The effect of metal ions on the lipolytic activity of Mycobacterium rubrum and Actinomyces streptomycini].

Hydrolysis of olive oil by intact cells of Mycobacterium rubrum 403 and "acetone" preparations of Actinomyces streptomycini 116 was found to be inhibited by the following ions: Ca2+, Mg2+, Mn2+, Ba2+, Co2+, Cd2+, Cu2+, Zn2+, Fe2+, Fe3+, Ni2+. Olive oil is hydrolyzed by the growing culture of Act. streptomycini 116 only in the presence of bivalent metal ions. The biosynthesis of lipase by Mycobatcerium rubrum 403 and Act. streptomycini 116 is increased twofold by magnesium ions. The biosynthesis of lipase by Act. stroptomycini 116 is stimulated also by calcium ions.

Actinomycetales↗