Microbiological and Enzymatic Production of Flavor and Fragrance Chemicals

Welsh, Frank W.; Murray, William D.; Williams, Robert

doi:10.3109/07388558909040617

Cited by 240 publications

(103 citation statements)

References 310 publications

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“…Likewise, its application in non-alcoholic beverages, ice creams, candy, baked goods, gelatins and puddings, chewing gums, cigarettes, and smokeless tobacco is reported (Welsh et al 1989). Although flavor esters are currently produced by chemical synthesis, the use of lipases offers environmental advantages and a reduction in energy consumption.…”

Section: Introductionmentioning

confidence: 99%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

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Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion (> 99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g -1 dry support and in a relatively short time (24 hrs) at 37ºC, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.

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Section: Introductionmentioning

confidence: 99%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

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“…Isoamyl acetate, also called isopentyl acetate, is the character impact compound of banana flavour and pear drops. It is one of the most highly employed compounds in the food industries with a production of 74 tonnes per annum 22 . The extracts of natural flavour esters from plant materials are often in short supply.…”

Section: Introductionmentioning

confidence: 99%

Production of Isoamyl Acetate from Sugar Beet Molasses by Williopsis saturnus var. saturnus

Yılmaztekin

Erten

Cabaroğlu

2008

Journal of the Institute of Brewing

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Three strains of Williopsis saturnus var. saturnus were employed for the production of natural isoamyl acetate (the character impact compound of banana flavour) using sugar beet molasses as the carbon source and batch cultivation at 25°C under anaerobic conditions. Of the three strains, strain HUT 7087 was the best producer of isoamyl acetate, producing 20.7 mg/L. Sugar beet molasses was deemed to be an acceptable carbon source for the production of this flavour compound.

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“…Phenylethanol, which has a rose-like aroma, is an important fragrance in the cosmetic industry (9,19) and possesses organoleptic characteristics that contribute to the quality of beverages and foods (19,22,52). While chemically synthesized phenylethanol is a valuable compound, phenylethanol that is synthesized biologically is 250-to 300-fold more expensive (17).…”

mentioning

confidence: 99%

Identification and Characterization of Phenylpyruvate Decarboxylase Genes in Saccharomyces cerevisiae

Vuralhan

Morais

Tai

et al. 2003

Appl Environ Microbiol

168

159

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Catabolism of amino acids via the Ehrlich pathway involves transamination to the corresponding ␣-keto acids, followed by decarboxylation to an aldehyde and then reduction to an alcohol. Alternatively, the aldehyde may be oxidized to an acid. This pathway is functional in Saccharomyces cerevisiae, since during growth in glucose-limited chemostat cultures with phenylalanine as the sole nitrogen source, phenylethanol and phenylacetate were produced in quantities that accounted for all of the phenylalanine consumed. Our objective was to identify the structural gene(s) required for the decarboxylation of phenylpyruvate to phenylacetaldehyde, the first specific step in the Ehrlich pathway. S. cerevisiae possesses five candidate genes with sequence similarity to genes encoding thiamine diphosphate-dependent decarboxylases that could encode this activity: YDR380w/ ARO10, YDL080C/THI3, PDC1, PDC5, and PDC6. Phenylpyruvate decarboxylase activity was present in cultures grown with phenylalanine as the sole nitrogen source but was absent from ammonia-grown cultures. Furthermore, the transcript level of one candidate gene (ARO10) increased 30-fold when phenylalanine replaced ammonia as the sole nitrogen source. Analyses of phenylalanine catabolite production and phenylpyruvate decarboxylase enzyme assays indicated that ARO10 was sufficient to encode phenylpyruvate decarboxylase activity in the absence of the four other candidate genes. There was also an alternative activity with a higher capacity but lower affinity for phenylpyruvate. The candidate gene THI3 did not itself encode an active phenylpyruvate decarboxylase but was required along with one or more pyruvate decarboxylase genes (PDC1, PDC5, and PDC6) for the alternative activity. The K m and V max values of the two activities differed, showing that Aro10p is the physiologically relevant phenylpyruvate decarboxylase in wild-type cells. Modifications to this gene could therefore be important for metabolic engineering of the Ehrlich pathway.

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Microbiological and Enzymatic Production of Flavor and Fragrance Chemicals

Cited by 240 publications

References 310 publications

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Production of Isoamyl Acetate from Sugar Beet Molasses by Williopsis saturnus var. saturnus

Identification and Characterization of Phenylpyruvate Decarboxylase Genes in Saccharomyces cerevisiae

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