We purified yeast-Iytic enzymes from Rarobacterfaecitabidus, a yeast-lytic coryneform bacterium isolated from a wastewater treatment system. The enzymesconsisted of one /?-l,3-glucanase and two proteases. Molecular weights of the two proteases and /M,3-glucanase were 35,000, 33,000, and 82,000 respectively by SDS polyacrylamide gel electrophoresis. The two proteases were serine proteases, which were inhibited by diisopropyl fluorophosphate or phenylmethylsulfonyl fluoride, and most active in alkaline pH. These proteases could decrease the turbidity of yeast suspensions. In this report, we described the purification and some characteristics of the two proteases and /M ,3-glucanase.

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A high-ethyl caproate-producing strain, Saccharomyces cerevisiae strain 3703-7, was isolated from cerulenin-resistant mutants of sake yeast. The strain produced a large amount of ethyl caproate when it was grown on a 15% glucose concentration and at 25C. A much higher yield of ethyl caproate was produced from sucrose or fructose than from glucose added as a substrate. On the other hand, glucose concentration and growth temperature were not effective for the production of ethyl caproate by the parent strain 3703. From these results, it was suggested that strain 3703-7 produces ethyl caproate, ethyl acetate, and isoamyl acetate from the apple pomace extract containing sugars composed of glucose, fructose, and sucrose. The strain 3703-7 was grown in the apple pomace extract containing 6. 4% and 10. 4% sugars at 25C. Ethyl caproate was produced in a much larger amount in the 10. 4% than the 6. 4% sugars. After 8 days of incubation in the pomace extract containing 10. 8% sugars at 25C, 5. 23%of ethanol was produced, and the production amounts of ethyl caproate, ethyl acetate and isoamyl acetate were 3. 12 ppm, 7. 13 ppm, and 0. 45 ppm, respectively. The distilled liquor had the flavor of alcohol containing 32. 3% ethanol, possessing a sweet aroma typical of ethyl caproate in addition to an apple flavor.

Effects of exogenousBt2cAMP and Bt2cGMP on the changes in lipase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, and invertase activities were investigated during the germination of pollen from Pinus densiflora Sieb. et Zucc. Both nucleotides cooperatively restored the lipase activity which was depressed by exogenous sucrose, but had no effect on the change in glucose-6-phosphate dehydrogenase activity. Either Bt2cAMPor Bt2cGMPpartially restored the glutamate dehydrogenase activity which was depressed by exogenous sucrose. Bt2cGMPlowered the invertase activity during germination, whereas Bt2cAMP reversed this depression. Using inhibitors of RNAand protein synthesis, we suggested that Bt2cAMPand Bt2cGMPcontrol the invertase activity at the transcriptional and translational levels, respectively.

Apple pomace was fractionated into the water-soluble and water-insoluble materials (apple pulp). The effective saccharification method of apple pulp using PECTINASE HL from Aspergillus sp. (PECase) and CELLULASE "ONOZUKA" 3S (CELase) from Trichoderma viride, was investigated in addition to a screening of favorable microorganism for lactic acid fermentation from Lactobacillus amylophilus (NBRC15881), Rhizopus oryzae (NBRC5384) and Kluyveromyces thermoteleran (AOK A0357-23). On the basis of the results, lactic acid production by R. oryzae from the mixture of water-soluble materials of apple pomace and the materials solubilized by hydrolysis of apple pulp with a mixture of PECase and CELase was carried out. Lactic acid was produced at a concentration of 572 g from 46.8 kg (wet wt.