Degradation of fructan obtained from timothy (Phleum pratense L.) by the following six species of bacteria isolated from sheep rumen was studied: Streptococcus bovis, Bacteroides ruminicola, Selenomonas ruminantium, Butyrivibrio fibrisolvens, Treponema bryantii and Treponema saccharophilum. The enzymatic activity of the bacteria was analysed by TLC. The highest activity was found in whole cells and in the strains B. fibrisolvens No. 3 and T. saccharophilum S.
A poly(1,4-alpha-D-galacturonide) lyase (EC 4.2.2.2) from the culture fluid of Lachnospira multiparus was purified about 20-fold. The optimum pH and temperature for enzyme activity were 8.0 and 40 degrees C. The enzyme required Ca2+ and was inhibited by EDTA; it preferred polygalacturonate as substrate, cleaving 1,4-alpha-glycosidic linkages randomly to form unsaturated galacturonates, mainly the unsaturated digalacturonate. Some properties of the crude and purified enzyme preparations are described. An exopolygalacturonase is also produced by this organism.
An extracellular pectinolytic enzyme produced by Butyrivibrio fibrisolvens isolated from the bovine rumen was studied. The enzyme had a pH optimum of 8.0 to 8.5 and was stimulated by Ca2+ and inhibited by EDTA. The products of pectinolysis had an absorption peak at 235 nm and reacted with thiobarbituric acid, indicating a lyase type of action. The enzyme cleaved the substrates terminally from the reducing end; action on poly- and oligogalacturonates resulted in the formation of an unsaturated trigalacturonate. The enzyme was classified as an exopectate lyase (EC 4.2.2.9). A pectinesterase was also produced by B. fibrisolvens but polygalacturonase was not detected.
Two strains of small spirochetes utilizing pectin as sole source of energy for growth were isolated from the rumen of cattle and partially characterized. The pectinolytic enzyme produced by one of the organisms was classified as a poly-1,4-aD -galacturonide lyase (EC 4.2.2.2). A pectinesterase (EC 3.1.1.11) was also produced.
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