Metabolism of geraniol in grape berry mesocarp of L. cv. Scheurebe: demonstration of stereoselective reduction, /-isomerization, oxidation and glycosylation

Luan, Fang; Mosandl, Armin; Münch, Andreas; Wüst, Matthias

doi:10.1016/j.phytochem.2004.12.017

Cited by 95 publications

(66 citation statements)

References 28 publications

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“…Extracellular sucrase, galactosidases as well as proteolytic enzymes, which are released from plant cells, may be of some importance for biotechnological application in the food and pharmaceutical research and industry (LUAN et al 2005;MIČIETA et al 2002;WATSON et al 2001;MATSUURA et al 2004;MUČAJI et al 2001). Sucrase could be used for biotransformation of sucrose to glucose and fructose (invert sugars) enabling the successive production of fructose containing a preparation suitable for the food industry and diabetics (SCHLEE, KLEBER 1991;MANSFELD et al 1992;ASANO 2003).…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…The data indicate a 91.5-92.0% intracellular and 8.0-8.5% extracellular distribution of the enzyme activity tested. The intracellular specific enzyme activity is 1.72-1.84 times higher.The production of extracellular glycosidases as well as proteolytic enzymes (BALASUBRAMANIAM et al 2005;LUAN et al 2005;MERTOVÁ et al 2002) that are released from plant cells might be of some importance for biotechnological applications in the food and pharmaceutical research and industry (SHIBANO et al 2004;WILLITS et al 2004;ASANO et al 2000; EL ASHRY et al 2000a,b,c;WATSON et al It is a very well-known fact that glycosidase inhibitors such as many mono-and bicyclic polyhydroxylated pyrrolides, piperidines and azepines (referred to as iminosugars or azasugars) have the potential as antiviral, anticancer and antidiabetic agents. Some of these inhibitors have already been put on the market for treatment of diabetes.…”

mentioning

confidence: 99%

“…The mechanisms of these effects have been studied extensively. Some of them are naturally occurring and owing to the pronounced biological activity of this class of compounds various synthetic routes have been designed for the syntheses of many of them (EL ASHRY et al 2000a,b,c;WATSON et al 2001;MATSUURA et al 2004).Extracellular sucrase, galactosidases as well as proteolytic enzymes, which are released from plant cells, may be of some importance for biotechnological application in the food and pharmaceutical research and industry (LUAN et al 2005;MIČIETA et al 2002;WATSON et al 2001;MATSUURA et al 2004;MUČAJI et al 2001). Sucrase could be used for biotransformation of sucrose to glucose and fructose (invert sugars) enabling the successive production of fructose containing a preparation suitable for the food industry and diabetics (SCHLEE, KLEBER 1991;MANSFELD et al 1992;ASANO 2003).…”

mentioning

confidence: 99%

“…These enzymes as well as galactosidases and proteases (MIČIETA et al 2002;MERTOVÁ et al 2002) are generally present in plants. They have not been used in biological processes until now (BALASUBRAMANIAM et al 2005;LUAN et al 2005;BILKA et al 2002).Due to its simplicity and reproducibility the method presented here could be useful for the detection of sucrase in plants and their enzymatic improvement.R e f e r e n c e s ASANO N., NASH R., MOLYNEUX R., FLEET G.W.J., 2000.Sugar mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application. Identifikácia sacharázy v kultivačnom médiu melóna ABSTRAKT: Sacharáza (kyslá solubilná) sa detegovala v kultivačnom médiu suspenzných kultúr dyne červenej (Citrullus vulgaris L.).…”

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confidence: 99%

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Identification of sucrase activity in cell suspension and culture medium of melon

Stano¹,

Mičieta²,

Barth³

et al. 2005

Hort. Sci. (Prague)

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ABSTRACT:The activity of (soluble acid) sucrase was detected in a culture medium of the cell suspension culture of watermelon (Citrullus vulgaris L.). A simple and rapid procedure for the identification and determination of extracellular sucrase from a culture medium of watermelon cell suspension cultures is described. Sucrose was used as a substrate for the determination of extracellular and intracellular activities of the enzyme. Intracellular activity was estimated from the cell suspension. The results show a 91.5-92.0% intracellular and 8.0-8.5% extracellular distribution of sucrase activity. The described method enables to carry out a rapid, simple and specific detection of extracellular sucrase in plants. 105 lus vulgaris cv. Samara as previously described by TILEMANN et al. (2003).Identification and determination of intra-and extracellular sucraseUsing sucrose as a substrate the intra-and extracellular activity of soluble acid sucrase was identified. Eight days old cell suspension cultures were used to determine the intracellular enzyme activity. The cells (5 g) were filtered and washed twice with 1,000 ml of distilled water. Soluble proteins were extracted by grinding the cells in a pre-cooled mortar using a ratio 1:2 (g/ml) of cells and Mc Ilvaine buffer pH 4.5 at 4°C. The homogenate was filtered through two layers of nylon cloth and centrifuged at 15,000 g at 4°C. For determinations of extracellular enzyme activity the cultivation medium (without cells) was used after centrifugation (15,000 g, 10 min at 4°C). Enzyme assayEnzyme activity was determined by a modified method of RUBIO et al. (2002) using sucrose as a substrate. The reaction mixture contained a suitable amount of enzyme (0.2-0.4 ml) and 0.4 mM sucrose in Mc Ilvaine buffer pH 4.5 in a final volume of 2 ml. Enzyme activity was determined at 30°C for 30 to 60 min. The control contained temperature-inactivated enzyme (100°C, 10 min). The enzyme activity was expressed in katals. Proteins were determined by the method of BRADFORD (1976) using bovine serum albumin as a standard protein. The glucose content released by the enzyme was determined by the method of TRINDER (1969). RESULTS AND DISCUSSIONSynthetic chromogenic substrates are very suitable for biochemical and histochemical studies of hydrolytic enzymes. In the last decades, several methods for the determination of hydrolytic enzymes have been developed. Various naturally occurring chromogenic substrates may be used for these purposes (KIM et al. 2002;MIČIETA et al. 2002). p-nitrophenyl-β-Dfructofuranoside and naphthyl-β-D-fructofuranoside were not synthesised and only a natural substrate -sucrose was used for the study of sucrase.Therefore only sucrose was used to study the activity of intracellular and extracellular (acid soluble) sucrase. The highest specific activity of the studied enzyme was recorded on day 8 of cultivation (Table 2) in undifferentiated cells. Homogenised cell suspension cultures and culture medium alone after 8-day cultivation were used to assay the activity of intrac...

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