Abstract: The present invention discloses a method for the enzymatic synthesis of a peptide. A protected peptide having a C-terminal carboxylate group or a protected, N-acyl amino acid having an alpha carboxylate group is reacted with a protected peptide having an N-terminal ammonium group or a protected amino acid having an alpha ammonium group in the presence of a condensation enzyme under conditions in which the carboxylate group and the ammonium group condense to form a protected, uncharged, peptide product. This peptide product is transported across a water-immiscible hydrophobic phase into an aqueous product phase and prevented from back diffusing across the water-immiscible hydrophobic phase. The peptide product can be converted, chemically or enzymatically, to a charged species that cannot back diffuse across the water-immiscible phase into the aqueous reaction phase.

Abstract: The present invention discloses a method for the enzymatic synthesis of a peptide. A protected peptide having a C-terminal carboxylate group or a protected, N-acyl amino acid having an alpha carboxylate group is reacted with a protected peptide having an N-terminal ammonium group or a protected amino acid having an alpha ammonium group in the presence of a condensation enzyme under conditions in which the carboxylate group and the ammonium group condense to form a protected, uncharged, peptide product. This peptide product is transported across a water-immiscible hydrophobic phase into an aqueous product phase. This peptide product is removed from the aqueous product phase to prevent back diffusion across the water-immiscible hydrophobic phase. Reverse osmosis and other separation techniques may be utilized to remove the peptide product.

Abstract: The present invention provides a method for the enzymatic synthesis of peptides accomplished by shifting the chemical equilibrium that exists in a reaction mixture between charged or ionized reacting amino acids and uncharged or non-ionized peptide product in the presence of a proteolytic enzyme such as thermolysin. The equilibrium is shifted by diffusion of the uncharged peptide product across an ion-rejection membrane which removes the uncharged peptide from the reaction mixture and preferably the diffused uncharged peptide is quickly converted to a charged species that cannot back-diffuse into the reaction mixture so that the uncharged peptide is effectively "pulled" across the membrane.

Abstract: The present invention provides a method for the enzymatic synthesis of peptides accomplished by shifting the chemical equilibrium that exists in a reaction mixture between charged or ionized reacting amino acids and uncharged or non-ionized peptide product in the presence of a proteolytic enzyme such as thermolysin. The equilibrium is shifted by diffusion of the uncharged peptide product across an ion-rejection membrane which removes the uncharged peptide from the reaction mixture and preferably the diffused uncharged peptide is quickly converted to a charged species that cannot back-diffuse into the reaction mixture so that the uncharged peptide is effectively "pulled" across the membrane.

Abstract: The present invention provides a membrane method for the enzymatic synthesis of peptides accomplished by shifting the chemical equilibrium that exists in a reaction mixture between charged or ionized reacting amino acids and uncharged or non-ionized peptide product in the presence of a proteolytic enzyme such as thermolysin. The equilibrium is shifted by diffusion of the unchanged peptide product across an ion-rejection membrane which removes the uncharged peptide from the reaction mixture and preferably the diffused uncharged peptide is quickly converted to a charged species that cannot back-diffuse into the reaction mixture so that the uncharged peptide is effectively "pulled" across the membrane. An enzymatic conversion of the uncharged species utilizing an esterase having proteolytic activity such as aminoacylase I is disclosed. Copermeating reactants can be separated from the product mixture and returned to the reaction mixture.

Abstract: The present invention relates to L-aspartyl-3-(bicycloalkyl)-L-alanine alkyl esters having high sweetness intensity, of the formula: ##STR1## wherein R.sup.1 is a substituted or an unsubstituted bicycloalkyl ring, said ring having 7 to 8 carbon atoms, the 2-position ring carbon atom is bound to the alamine moiety, the two carbon atoms of the ring that are vicinal to the 2-position carbon are each substituted by a hydrogen or lower alkyl, the total number of alkyl groups bound to the vicinal carbons is less than three, and R.sup.2 is methyl. The "2R" configuration enantiomers of the R.sup.1 group are especially preferred. In preferred embodiments of the invention, R.sup.1 is a bornyl, camphanyl, norbornyl, 1-methylnorbornyl, 3-methylnorbornyl, 7,7-dimethylnorbornyl, bicyclo [2.2.2] octyl, or pinanyl ring. The compounds of the invention, or edible salts thereof, can be used for sweetening edible products such as foods and beverages.

Abstract: Substituted pyrazinium compounds having at least one polar group such as hydroxyl, carboxyl, carbamido or sulfonoxy can act as high energy electron carriers in photosynthetic processes such as those employing chlorophyll and a reduction enzyme. Such processes with the pyrazinium compounds can produce ammonia and hydrogen.

Abstract: The sunlight stability of anthocyanic pigments in mixtures, especially foods, may be enhanced by including in the mixture a photoprotective agent selected from the group consisting of sulfonated polyhydroxyflavonols, poly(hydroxyalkyl) flavonols, sulfonated polyhydroxyflavones, sulfonated polyhydroxyiso-flavones, and sulfonated aurones.

Abstract: Disclosed herein is a process for reducing the tendency of the pigment rubrolone to fade upon exposure to direct sunlight wherein the pigment is combined with quercetin-5'-sulfonate. Pigment compositions comprised of rubrolone and quercetin-5'-sulfonate as well as food compositions containing these components are also disclosed.

Abstract: A novel color-stable food product containing anthocyanin or anthocyanidin pigments and containing bio-available vitamin C. The novel food may be produced as the product of an improved food production process wherein the improvement comprises providing the bioavailable vitamin C in the form of an enolic OH substituted derivative of ascorbic acid selected from the group consisting of inorganic esters, aliphatic or alicyclic esters, and O-alkyl ethers of ascorbic acid.

Abstract: Method for preparing a 3-deoxy-5-hydroxyanthocyanidin salt having a 4' and/or 7 OH substituent from a corresponding acylated flavanone, by (1) reducing the acylated flavanone in a solvent medium by reaction with an alkali borohydride to form a corresponding flavan not having an OH substituent at the 4 position, and (2) oxidizing the flavan or an acylated or hydrolyzed derivative of the flavan in an organic solvent medium by reaction with a halogenated benzoquinone in the presence of a strong acid and water. Suitable acylated flavanones include acetylated natural flavanones, especially acetylated naringenin and hesperetin.