@article { ISI:000209465100066,
	title = {Oxidoreductase from {\textquoteleft}Alphonso{\textquoteright} mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls},
	journal = {SpringerPlus},
	volume = {2},
	year = {2013},
	month = {OCT},
	pages = {494},
	publisher = {SPRINGER INTERNATIONAL PUBLISHING AG},
	type = {Article},
	address = {GEWERBESTRASSE 11, CHAM, CH-6330, SWITZERLAND},
	abstract = {<p>Two furanones, furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone), are important constituents of flavor of the Alphonso cultivar of mango (Mangifera indica). To get insights into the biosynthesis of these furanones, we isolated an enone oxidoreductase gene from the Alphonso mango. It has high sequence similarity to an alkenal/one oxidoreductase from cucumber (79\% identity) and enone oxidoreductases from tomato (73\% identity) and strawberry (72\% identity). The complete open reading frame was expressed in E. coli and the (his) 6-tagged recombinant protein was purified by affinity chromatography. The purified protein assayed with NADH as a reducing agent converted D-fructose-1,6-diphosphate into furaneol, the immediate precursor of mesifuran. The enzyme was also able to convert two highly reactive carbonyls, 3-buten-2-one and 1-penten-3-one, produced by lipid peroxidation in plants, into their saturated derivatives. Expression profiling in various ripening stages of Alphonso fruits depicted an expression maxima at 10 days after harvest stage, shortly before the appearance of the maximum amount of furanones (completely ripe stage, 15 days after harvest). Although no furanones were detected at the 0 day after harvest stage, significant expression of this gene was detected in the fruits at this stage. Overall, the results suggest that this oxidoreductase plays important roles in Alphonso mango fruits.</p>},
	keywords = {Detoxification, Enone oxidoreductase, Flavor, Mangifera indica, Ripening},
	issn = {2193-1801},
	doi = {10.1186/2193-1801-2-494},
	author = {Kulkarni, Ram and Chidley, Hemangi G. and Deshpande, Ashish and Schmidt, Axel and Pujari, Keshav and Giri, Ashok P. and Gershenzon, Jonathan and Gupta, Vidya}
}
@article {49406,
	title = {Aroma Alchemy: uridine diphosphate-dependent glycosyltransferases mediated regulation of fruit aroma and flavor biosynthesis},
	journal = {Phytochemistry Reviews},
	year = {2024},
	month = {DEC},
	type = {Review; Early Access},
	abstract = {<p>
	The aroma compounds contribute to fruits flavor, taste, and nutritional value. These compounds include various chemical classes such as terpenoids, lactones, ketones, esters, acids, alcohols, and their derivatives. Uridine diphosphate-dependent glycosyltransferases (UGTs) modify these compounds by covalently adding one or multiple sugar molecules. This glycosylation process converts volatile, unstable, and hydrophobic aroma compounds into hydrophilic, stable, and slow-releasing reservoirs of fruit flavor. The diversity and spatio-temporal expression patterns of UGTs play a crucial role in forming a wide range of glycosylated aroma compounds. This review focuses on aroma-related compounds in both free and glycosylated-bound forms found in commercial vital fruits. We discuss various fruit-specific UGTs and their role in the glycosylation of aroma compounds. Based on structural and functional information on UGTs, we have assessed sugar donor specificity and the residues responsible for the same. Moreover, phylogenetic analysis of characterized UGTs provides insights into their substrate preferences. We also surveyed the expression dynamics of UGTs during fruit ripening, as the switching between aglycon and glycosylated-bound forms of aroma compounds significantly impacts fruit quality. Potential applications of UGTs in the food and fragrance industry have been discussed. The information reviewed could be beneficial for developing novel methods for flavor manipulation of commercially important glycosides derived from natural resources.</p>
},
	keywords = {Aroma, Flavor, Fruit, Glycoconjugates, Glycosyltransferase, Volatile compounds},
	issn = {1568-7767},
	doi = {10.1007/s11101-024-10049-7},
	author = {Vare, Tejas B. and Joshi, Rakesh S. and Giri, Ashok P.}
}
