Abstract: An immunopropylactic and immunotherapeutic agent comprising human interleukin 2 of human cellular origin is disclosed along with a method of producing the agent.

Abstract: Purine-arabinosides and a method for making purine-arabinosides are disclosed. The method comprises contacting an arabinose donor and a purine source in the presence of an effective amount of enzyme produced by a bacterium and capable of transarabinosylation from the arabinose donor to the purine source, whereby a 9-(.beta.-D-arabinofuranosyl)-purine is produced.

Abstract: A method is provided for producing a peptidase capable of substantially completely hydrolyzing protein into its constituent amino acids which comprises culturing a strain of filamentous fungus, belonging to one of the species Aspergillus oryzae and Aspergillus soyae and characterized in that said strain is capable of producing said peptidase, in a nutrient culture medium containing at least one substrate selected from the group consisting of a fatty acid having 14, 16, 18 or 20 carbon atoms and a derivative of said fatty acid, and recovering said peptidase from said culture medium. It is particularly effective to use a combination of a sugar ester of a fatty acid and a vegetable oil as substrates in a liquid culture medium.

Abstract: D-.alpha.-amino acids are produced by contacting a 5-substituted hydantoin with an effective amount of an enzyme capable of converting the 5-substituted hydantoin to the D-.alpha.-amino acid produced by a microorganism in an aqueous medium at a pH in the range of 4 to 9, the microorganism being capable of utilizing the D-isomer of the 5-substituted hydantoin as the sole nitrogen source, but substantially incapable of utilizing the L-isomer of the 5-substituted hydantoin as the nitrogen source and the substituent of the 5-position being such that upon reaction with the enzyme, an optically active D-.alpha.-amino acid isomer is produced; and recovering the D-.alpha.-amino acid which accumulates in the aqueous medium.

Abstract: A method for producing 4-formyl-2-amino-butyric acid(FABA), which comprises: culturing a mutant capable of producing FABA and belonging to the genus Brevibacterium or Corynebacterium in a culture medium until a substantial amount of FABA has accumulated in the culture medium, and recovering the accumulated FABA from the culture medium.

Abstract: 2-Amino-(2)-thiazoline-4-carboxylic acid is prepared by dehydrochlorinating S-(.beta.-carboxy-.beta.-chloroethyl) isothiourea by adding it to an aqueous medium maintained at a pH ranging from 5.5 to 7.5 with an alkali.

Abstract: Method for the production of substituted sulfur containing L-amino acids by contacting .beta.- or .gamma.-substituted amino acids in an aqueous medium containing methioninase together with the precursor of the substituent.

Abstract: Alpha-amylases which have optimum activity between pH 6.5 to 8 and between pH 9.0 to 11.5 at 40.degree. C are produced by culturing strains of Bacillus subtilis on a nutrient medium under aerobic conditions. Some of the alpha amylases are effective in hot and alkaline detergent solutions containing chelating agents.

Abstract: L-amino acids are produced by fermenting a hydantoin compound with Flavobacterium aminogenes or its enzymes.

Abstract: A method for producing L-cysteine and/or L-cystine which comprises:A. holding 2-amino-thiazoline-4-carboxylic acid in an aqueous solution at a pH of 5 to 11 in the presence of an effective amount of enzyme produced by a microorganism; said enzyme being capable of converting the 2-amino-thiazoline-4-carboxylic acid to L-cysteine and/or L-cystine, and said microorganism being capable of growing in a medium containing 2-amino-thiazoline-4-carboxylic acid as a nitrogen source; andB. recovering the L-cysteine and/or L-cystine formed from said aqueous solution.

Abstract: Some strains of Cladosporium produce highly active peptidase. The peptidase can liberate most amino acids from proteins in high yields.

Abstract: A decarboxylase in cells of Micrococcus strains converts tryptophan, phenylalanine, and substitution products thereof to the corresponding phenyl- and indolylethylamines. The enzyme can be recovered in pure state from the microorganisms, but cells and cell material are effective enzyme sources in the decarboxylation reaction.