Abstract: The present invention is directed to recombinant plant viral nucleic acids and to hosts infected thereby. The recombinant plant viral nucleic acids comprise a native plant viral subgenomic promoter, at least one non-native plant viral subgenomic promoter, a plant viral coat protein coding sequence, and optionally, at least one non-native nucleic acid sequence to be transcribed or expressed in the infected host plant. The recombinant plant viral nucleic acids are stable, capable of systemic infection and capable of stable transcription or expression in the plant host of the non-native nucleic acid sequences.

Abstract: The present invention relates to a nucleic acid sequence that encodes a fusion enzyme of tyrosinase and a tyrosinase activator protein. Further, the present invention also relates to the amino acid sequence which is encoded by the nucleic acid sequence of the fusion enzyme. The fusion enzyme may also include a linker positioned between the amino acid sequences of the tyrosinase and the tyrosinase activator protein. Still further, the present invention also relates to a vector useful for introducing the nucleic acid sequence encoding the fusion enzyme into an organism. Still further, the present invention relates to melanins made by the fusion enzyme and a method for making melanins using the fusion enzyme.

Abstract: The present invention relates to the production of three (3) distinct savory flavor types of dehydrated mushrooms: (1) a light-colored material with strong mushroom flavor, (2) a tan-colored material with a meaty, buttery and savory flavor and (3) a dark-colored material with a beefy, meaty, chocolate flavor. All three products exhibit "umami" or monosodium glutamate (MSG)-like mouthfeel and flavor synergy. The mushrooms are produced using specialized nutrient additives, controlled growing conditions and specialized dehydration protocols.

Abstract: Two novel genomic clones, ZZA1 and ZZA2, were isolated which encode for Pichia pastoris alcohol oxidase isozymes. The 5' non-coding region of ZZA1 contains common structural features involved in the transcription and translation of eukaryotic genes. Comparison of the nucleotide sequences of the ZZA1 and AOX15' noncoding regions showed that they are 66% similar to each other.The rice .alpha.-amylase gene OS103 was placed under the transcriptional control of the ZZA1 promoter. The nucleotide sequences of ZZA1 and other methanol-regulated promoters were analyzed. A highly conserved sequence (TTGNNNGCTTCCAANNNNNTGGT) (SEQ ID NO: 2) was found in the 5' flanking region. A yeast strain containing the ZZA1-OS103 fusion and secreting biologically active .alpha.-amylase into the culture media while converting starch to ethanol was produced. The ZZA1 and ZZA2 regulatory sequences may be used to contol the expression of other heterologous proteins in multiple yeast species.

Abstract: A process for the in vitro production of chemically modified polyphenolic polymer (PPP). First, stable, highly active extracellular tyrosinase is produced from genetically transformed microorganism such as Streptomyces antibioticus. The tyrosinase is then incubated with a reaction substrate such as 1-tyrosine, hydrolyzed protein, or an oligopeptide in combination with 1-tyrosine. The ratio of the oligopeptide/tyrosine combination as well as variation in the concentration of tyrosinase can be used to modify the color, the molecular size, and the spectral absorbance properties of the PPP produced. Alternatively, or additionally, oxidants such as hydrogen peroxide or hypochlorite can be used to modify the color of the PPP, regardless of the method used to produce the PPP, and the PPP can subsequently be fractionated using molecular weight cut-off ultrafiltration. Organic solvents can also be used in the method of making PPP to produce PPPs having variable but reproducible physical properties.

Abstract: A process for the in vitro production of chemically modified polyphenolic polymer (PPP). First, stable, highly active extracellular tyrosinase is produced from genetically transformed microorganism such as Streptomyces antibioticus. The tyrosinase is then incubated with a reaction substrate such as l-tyrosine, hydrolyzed protein, or an oligopeptide in combination with l-tyrosine. The ratio of the oligopeptide/tyrosine combination as well as variation in the concentration of tyrosinase can be used to modify the color, the molecular size, and the spectral absorbance properties of the PPP produced. Alternatively, or additionally, oxidants such as hydrogen peroxide or hypochlorite can be used to modify the color of the PPP, regardless of the method used to produce the PPP, and the PPP can subsequently be fractionated using molecular weight cut-off ultrafiltration. Organic solvents can also be used in the method of making PPP to produce PPPs having variable but reproducible physical properties.