A taxonomic study of the genus Chaetomium in Japan is prepared under the modern criteria. Twenty-four species are described and illustrated, of which fifteen species are isolated from natural sources in the area. The new species, C. gracile, is described. Eleven species are reported for the first time in Japan. These are C. indicum Corda, C. aureum Chivers, C. trilaterale Chivers, C. fusiforme Chivers, C. torulosum Bain., C. murorum Corda, C. atrobrunneum Ames, C. olivaceum Cooke et Ell., C. bostrycodes Zopf, C. cochliodes Palliser, and C. spirale Zopf. A key to the species is included.
A species of Daphnia (water-flea), Moina macropa, was grown (under a dark-aerobic condition) using fresh cells of Chlorella ellipsoidea as a sole organic nutrient. After 45 hours of culture at 25° in the dark, the weight gain in Daphnia in percentage of the weight loss in Chlorella was found to be 30-33%, and the amount of nitrogen assimilated by Daphnia in percentage of the amount of nitrogen in Chlorella consumed was calculated to be 38-42%. These values were compared with some relevant data reported in the literature, and it was inferred that the culturing of Daphnia with Chlorella may probably be a most efficient syystem for coverting plant protein into animal protein.
(1) It was ascertained that acetic, succinic, glycolic, pyruvic and α-ketoglutaric acids are derived from K-5-ketogluconate as the catabolic products in the presence of a trace of glucose under aerobic condition by intact cell suspension of Acetobacter suboxydans ATCC 621. (2) The yield of α-ketoglutaric acid was about 3% of 5-ketogluconic acid supplied as the substrate and the former acid produced did not undergo further oxidation. (3) It was ascertained that dried cells of this organism which were capable of oxidizing 5-ketogluconic acid did not oxidize the members of the tricarboxylic acid cycle and related compounds except oxalacetic acid. This result suggests that tricarboxylic acid cycle may not be operative in the degradation processes of 5-ketogluconic acid. (4) Glycolaldehyde was oxidized by this organism quantitatively but glycolic acid produced could not be oxidized further. (5) L-Tartaric acid could not be oxidized even though a small amount of glucose was added into the reaction system.
1. As a strain of forming β-1, 3′-xylan splitting enzyme, Chaetomiumglobosum A2 was selected out. 2. The enzyme activities in the shaking cultural medium toward two xylans, β-1, 3′- and β-1, 4′-xylans, were observed with the growth of Ch. globosum A2. The maximum activity of β-1, 3′-xylan splitting enzyme was found after 5 days incubation in semi-synthetic medium. From a comparative test on the forming patterns of β-1, 3′- and β-1, 4′-xylan splitting enzymes with the cultivation, these enzymes were found to be independent of each other. 3. β-1, 3′-xylan splitting enzyme was prepared from the cultural broth of the mold in a highly purified state which shows a 100-fold specific activity of that of starting sample. The purified preparation did not show any activities of β-1, 4′-xylanases, cellulase and amylases. 4. β-1, 3′-xylan in a relatively low concentration was almost completely hydrolyzed by the enzyme and converted into xylose and small amount of glucose. Oligo-saccharides could not be detected as intermediary and end products by paperchromatography. 5. When various β-1, 3′-xylo-oligosaccharides were used as substrates, sugars of the higher degree of the polymerization were more readily hydrolyzed than the lower ones. And xylose and xylobiose were found to be the end products from oligo-sugars. The enzyme could not hydrolyzed xylobiose. In these cases the formation of various oligosaccharides could be demonstrated as intermediary products. 6. From the above findings, β-1, 3′-xylan splitting enzyme prepared here should be classified into xylanase and we propose the name "EXO-β-1, 3′-XYLANASE" for it.
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Edited and published by : Applied Microbiology, Molecular and Cellular Biosciences Research Foundation/Center for Academic Publications Japan Produced and listed by : TERRAPUB, Center for Academic Publications Japan/Shobi Printing Co., Ltd. (-Vol.60,No12), Center for Academic Publications Japan/InternationalAcademic Printing Co., Ltd.(-Vol.54,No1)