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Fragmentation of forest habitat has negative effects on arboreal mammals, compromising their natural dispersal and foraging movements. This paper describes an evolving series of mitigation measures aimed at creating cost-effective continuity pathways for arboreal mammals in Japan. The projects have focused on the endemic Japanese dormouse (Glirulus japonicus) a scarce, but popular and iconic species which provides an effective vehicle for environmental education and public engagement.

An organic photochemical was crystallized in batches-wise both in laboratory and industrial crystallizers. In the laboratory, crystals were produced at different stirring speeds using a 1 L crystallizer, and the centrifugal filtration tests were conducted for the slurries that were obtained slurries. The average specific resistance was reduced much more than expected from the Kozeny-Carmann equation. This suggested that the a change occurred in the channel structure occurred in the cake composed of the crystalline particles that were obtained. Based on the above laboratory tests, batch crystallization with a low-speed intermittent stirring technique was applied for an actual crystallizer. The filtration time was reduced in the actual plant to about 1/10 of that of the previous conventional stirring crystallization.

The gene tanLpl, encoding a novel tannase enzyme (TanLpl), has been cloned from Lactobacillus plantarum ATCC 14917(T). This is the first report of a tannase gene cloned from a bacterial source other than from Staphylococcus lugdunensis, which has been reported elsewhere. The open reading frame of tanLpl, spanning 1410 bp, encoded a 469-amino-acid protein that showed 28.8% identity to the tannase of S. lugdunensis with several commonly conserved sequences. These sequences could not be found in putative tannases reported for other bacteria and fungi. TanLpl was expressed in Escherichia coli DH5alpha from a pGEM-T expression system and purified. SDS-PAGE analysis indicated that purified TanLpl was a monomer polypeptide of approximately 50 kDa in size. Subsequent enzymatic characterization revealed that TanLpl was most active in an alkaline pH range at 40 degrees C, which was quite different from that observed for a fungal tannase of Aspergillus oryzae. In addition, the Michaelis-Menten constant of TanLpl was markedly lower than that of A. oryzae tannase. The evidence suggests that TanLpl should be classified into a novel family of tannases.