Abstract: This invention relates to an improvement in a method for manufacturing dipeptides by coupling N-blocked aspartic acid and a phenylalanine lower alkyl ester in a medium containing a water-miscible organic solvent mixture in the presence of an immobilized metallo-protease so that a continuous reaction is established with stable enzyme activity.

Abstract: A novel E. coli strain which can produce L-phenylalanine and is resistant to high osmotic pressure and a process for producing L-phenylalanine by use of the novel E. coli (KCCM 10,016) are disclosed.

Abstract: Compositions containing L-aspartate or L-asparagine for use as additives to foods, soft drinks, vitamins, and the like are described. A method for preventing ethanol toxicity in a human subject is also provided.

Abstract: A process for the preparation of .alpha.-L-aspartyl-L-phenylalanine methyl ester in high yield, which comprises the steps of esterifying L-phenylalanine with methanol while undergoing continuous evaporation to remove the water formed during esterification, coupling the produced L-phenylalanine methyl ester with N-formyl-L-aspartic anhydride, deformylating the produced N-formyl-L-aspartyl-L-phenylalanine methyl ester, crystallizing the formed .alpha.-L-aspartyl-L-phenylalanine methyl ester as .alpha.-L-aspartyl-L-phenylalanine methyl ester hydrochloric acid salt, recovering the first .alpha.-L-aspartyl-L-phenylalanine methyl ester hydrochloric acid salt, esterifying .alpha.-L-aspartyl-L-phenylalanine in the filtrate to produce the second .alpha.-L-aspartyl-L-phenylalanine methyl ester, and combining the first and second .alpha.-L-aspartyl-L-phenylalanine methyl ester product.

Abstract: A novel E. coli (KCCM 10,013) which can produce high yields of L-phenylalanine and a method for production of L-phenylalanine by recombinant E. coli which may be transformed with a novel plasmid pMW16 containing two promoters and a temperature-sensitive repressor for expressing a pheA gene and an aroF gene wherein chorismate mutase p-prephenate dehydratase is coded for by the pheA gene and 3-deoxy-D-arabinoheptulosonate.7-phosphate synthase is coded for by the aroF gene.

Abstract: An immobilized fructosyltransferase enzyme is prepared by providing a porous or macroporous anion exchange resin having at least 1.0 m.sup.2 /g of internal surface, at least 0.1 ml/g of total porous volume, a spherical radius of 20-2,000 angstroms, and a nominal ion-exchange capacity of at least 1.0 meq./g of wet resin, adding to the ion-exchange resin a solution of fructosyltransferase enzyme derived from a microorganism of the genus Aureobasidium, Aspergillus, Fusarium, or Gloeosporium at a pH value of about 3-8, filtering and wind-drying the absorbed resin, and storing it in a cool place. A bifunctional cross-linking agent may be present in the solution of fructosyltransferase enzyme.

Abstract: A method for relieving fatigue in a mammalian recipient by administering to the mammalian recipient an effective amount of monosodium L-glutamate or a health food composition thereof.

Abstract: An E. Coli which can produce phenylalanine and which has an optimum phenylalanine production capability at a temperature of 30.degree. to 35.degree. C., and a process for preparing L-phenylalanine by use of the novel E. coli MWPEC 12-45 (ATCC 67460).

Abstract: An E. coli which can produce phenylalanine and which has an optimum phenylalanine production capability at a temperature between 30.degree. C. and 35.degree. C., and a process for preparing L-phenylalanine by use of the novel E. coli. The novel E. coli is designated MWPEC 13-60 (ATCC 67459).

Abstract: A process for purification and recovery of phenylalanine from a microbial fermentation broth containing phenylalanine which comprises providing a zinc salt of phenylalanine at a pH of 7-9, adding acid at a pH of 4-7, and separating precipitated phenylalanine.