02343nas a2200217   4500008004100000022001400041245012900055210006900184260000800253520157400261653001001835653001101845653001001856653002001866653002401886653002301910100002001933700002201953700002001975856013001995       2024                        eng d  a1568-776700aAroma Alchemy: uridine diphosphate-dependent glycosyltransferases mediated regulation of fruit aroma and flavor biosynthesis0 aAroma Alchemy uridine diphosphatedependent glycosyltransferases   cDEC3 a<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>
10aAroma10aFlavor10aFruit10aGlycoconjugates10aGlycosyltransferase10aVolatile compounds1 aVare, Tejas, B.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/aroma-alchemy-uridine-diphosphate-dependent-glycosyltransferases-mediated-regulation-fruit02434nas a2200289   4500008004100000022001400041245013600055210006900191260000900260300000800269490000700277520149200284653001601776653001201792653002001804653001701824653001501841653001401856100001501870700001801885700002001903700002101923700002801944700002301972700002601995856012302021       2025                        eng d  a0301-485100aComprehensive in vitro and in silico assessment of eugenol glycoconjugates against azole and amphotericin B resistant Rhizopus spp.0 aComprehensive in vitro and in silico assessment of eugenol glyco  cJUN   a5890 v523 a<p>
	Background Rhizopus spp. is a major cause of mucormycosis, a severe infectious disease with high morbidity and mortality. Treatment is challenging due to rising antifungal resistance. Glycosylation is a crucial technique for enhancing the properties of phenolic compounds like eugenol. The present study aims to examine the antifungal efficacy of eugenol glycoconjugates against azole and amphotericin B-resistant Rhizopus isolates. Methods and results Out of 50 soil samples, 12 isolates belonging to Mucorales were obtained, of which 7 were identified as Rhizopus spp. via 18S ITS sequencing. Antifungal susceptibility testing (AST) revealed that all Rhizopus isolates were resistant to amphotericin B (MIC &gt; 1 mu g/mL). Most isolates also showed resistance towards posaconazole (MIC &gt; 1 mu g/mL) and itraconazole (MIC &gt; 2 mu g/mL). AST of eugenol glycoconjugate (coded 6g) showed efficacy against resistant Rhizopus isolates, with MIC values ranging from 6.25 mu g/mL to 25 mu g/mL. Flow cytometry confirmed its fungicidal activity, correlating with MIC data. Compound 6g significantly reduced conidial germination within 24 h and exhibited no cytotoxicity on A549 lung cancer cells. In-silico analysis revealed a negative binding affinity of compound 6g for the spore coat protein CotH3, which could be a potential antifungal target. Conclusion Compound 6g could be an potential antifungal molecule against resistant Rhizopus spp, which requires further studies.</p>
10aAntifungals10aEugenol10aGlycoconjugates10aMucormycosis10aResistance10aVirulence1 aSen, Pooja1 aGupta, Lovely1 aChauhan, Aastha1 aGoswami, Lakshmi1 aBhattacharya, Asish, K.1 aSengupta, Abhishek1 aVijayaraghavan, Pooja  uhttps://library.ncl.res.in/content/comprehensive-vitro-and-silico-assessment-eugenol-glycoconjugates-against-azole-and02606nas a2200265   4500008004100000022001400041245009700055210006900152260000800221300001100229490000800240520174200248653001601990653001202006653001402018653002002032653005502052100001602107700001802123700001702141700002102158700002102179700001602200856012402216       2026                        eng d  a0981-942800aPhenylpropanoid-specific glycosyltransferases from mango and their potential role in defense0 aPhenylpropanoidspecific glycosyltransferases from mango and thei  cMAR  a1111370 v2323 a<p>
	Alphonso mango (Mangifera indica cv. Alphonso) is a cornerstone of India's fruit industry due to its distinct aroma and shelf-life characteristics. The uridine diphosphate-dependent glycosyltransferases (UGTs) play a crucial role in stabilising aroma and defense-related specialised metabolites in fruits. The present study explores the potential role of UGTs during mango ripening and Colletotrichum gloeosporioides infection. Gene expression analysis indicated that UGTs showed dynamic expression in skin and pulp during ripening. Phylogenetic analysis revealed substrate-driven divergence of UGTs, with MiUGT92A14 and MiUGT95B15 forming distinct clades associated with flavonoid glycosylation. Recombinant UGTs showed a higher preference for UDP-glucose, which is corroborated by the high accumulation of UDP-glucose during ripening. Furthermore, it was observed that MiUGT92A14 prefers phenolic acids as substrates, while MiGT95B15 shows flavonoid specificity. Spore germination assays demonstrated that both aglycones and their glycosylated derivatives suppressed early fungal morphogenesis, supporting a role for UGT-mediated glycosylation in maintaining defense-related metabolites in a bioactive yet non-toxic form during fruit ripening. Additionally, Colletotrichum gloeosporioides inhibition assays demonstrated that glycosylated products of selected UGTs exhibited equal or enhanced antifungal activity compared with their aglycone forms, indicating that glycosylation promotes the safe accumulation of antifungal compounds by reducing aglycone toxicity to the plant. These findings suggest that glycosylation of specific metabolites is a key for ripening process and to potentiate defence against fungal pathogen.</p>
10aAnthracnose10adefense10aFlavonoid10aGlycoconjugates10aUridine diphosphate-dependent glycosyl-transferase1 aVare, Tejas1 aJoshi, Rakesh1 aLiao, Jieren1 aHoffmann, Thomas1 aSchwab, Wilfried1 aGiri, Ashok  uhttps://library.ncl.res.in/content/phenylpropanoid-specific-glycosyltransferases-mango-and-their-potential-role-defense