Degradation of extracellular beta-(1,3)(1,6)-D-glucan by Botrytis cinerea

Article Abstract:

Botrytis cinerea produces an extracellular beta-D-glucan termed cinerean. An investigation was conducted to determine B. cinerea cinerean-degrading ability, possible cleavage products and enzyme localization. The results showed that B. cinerea does degrade extracellular cinerean, which is cleaved at the beta-1,3-linkage to produce glucose and gentiobiose. Gentiobiose is further cleaved by another hydrolytic step. The enzymes involved in these steps, beta-1,3-glucanase and gentiobiase, are localized in the cell wall.

Microbial polysaccharides, Glucans, Botrytis

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Inhibition of purified isocitrate lyase identified itaconate and oxalate as potential antimetabolites for the riboflavin overproducer Ashbya gossypii

Article Abstract:

Research on cultures of the riboflavin-producing fungus Ashbya gossypii during growth on soybean oil showed a specific isocitrate lyase of 0.17 U (mg protein) super -1. Enzyme activity could not be discerned during growth on glucose. This indicates a regulation. A 108-fold purification of the enzyme was achieved via ammonium sulphate fractionation, gel filtration and cation-exchange chromatography. The enzyme's pH optimum for the isocitrate cleavage was 7.0, and the K sub m for threo-DL-isocitrate was 550 micro M.

Fungi, Pathogenic, Pathogenic fungi, Vitamin B2, Riboflavin, Antimetabolites

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Glutamate dehydrogenase is not essential for glutamate formation by Corynebacterium glutamicum

Article Abstract:

The role of glutamate dehydrogenase (GDH) in the synthesis of glutamate and growth of Corynebacterium glutamicum was investigated by comparing the effects of mutations resulting in either GDH inactivity or GDH overproduction. The results showed that GDH is not essential for glutamate synthesis or secretion in C. glutamicum. The role of GDH is confined to its regulatory function in the GS/GOGAT system.

Bacteria, Glutamate, Dehydrogenases, Oxidoreductases

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