modifies histidine residues and inactivates the enzyme, pseudo first order kinetics. When the histidine modification is reversed by hydroxylamine treatment, 79% of the activity is restored
modifies tryptophan residues and inactivates the enzyme, loss of LGTase activity by NBS treatment is partially protected by pre-incubating the enzyme with excess limonin
inactivation of the enzyme following modification of carboxyl and imidazole moieties is a consequence of a loss in substrate binding and catalysis in the glucosyltransfer reaction. No inhibition by serine modifiying diisopropyl fluorophosphate and cysteine modifying 4-chloromercuribenzoate and iodoacetamide
at an acidic pH the D-ring of the substrate that should be in an open form is closed and glycosylation does not occur. The decrease in activity at acidic pH also indicates that an essential residue participates in catalytic functioning while in the unprotonated state
enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde (Chito-GA-LGTase) and enzyme immobilized covalently on cellulose carbonate (Ce-Ca-LGTase)
the genotype of the CitLGT locus in navel orange is homozygous for CitLGT-1 (CitLGT-1/CitLGT-1), whereas. The levels of non-bitter limonoid glucosides in navel orange fruit are quite low at the early-to mid-developmental stage due to a defective CitLGT-2
limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice
pH 7.5, 30 min, free enzyme retains 55% of the activity, enzyme immobilized ionically on DEAE-Toyopearl retains 80% of the activity, enzyme immobilized covalently on cellulose carbonate retains 45% of the activity, enzyme immobilized covalently on chitosan cross-linked with gluteraldehyde retains 40% of the activity
gene SLLGT, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli and in Pichia pastoris
Limonoid glucosyltransferase is an enzyme that catalyzes the conversion of bitter limonoid into non-bitter limonoid glucoside while retaining the health benefit of limonoids in the juice. The immobilization of this enzyme in a column can solve the juice bitterness problem
whether the CitLGT-2 is present or not, is a useful molecular indicator for predetermining the levels of accumulation of non-bitter limonoid glucosides at the early- to mid-developmental stages of Satsuma mandarin and navel orange fruits. These molecular indicators will make it possible to characterize fruit traits at the seedling stage, resulting in the marker-assisted selection of hybrid progenies to predetermine whether they will accumulate non-bitter limonoid glucosides
whether the CitLGT-2 is present or not, is a useful molecular indicator for predetermining the levels of accumulation of non-bitter limonoid glucosides at the early- to mid-developmental stages of Satsuma mandarin and navel orange fruits. These molecular indicators will make it possible to characterize fruit traits at the seedling stage, resulting in the marker-assisted selection of hybrid progenies to predetermine whether they will accumulate non-bitter limonoid glucosides
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
gene sequence of limonoid UDP-glucosyltransferase in citrus fruits with different bitterness do not vary but the pattern of expression, delayed bitterness is related to delay in expression of the limonoid glucosyltransferase gene
limonoid glucosides are important compounds not only for the processing industry but also for the consumer, bitterness due to limonoids is an important economic problem in commercial citrus juice production, limonoid aglycones are converted to nonbitter glucosides by the GTase, enhancement of the limonoid GTase activity through genetic engineering could reduce aglycone concentration, insertion of a gene encoding for GTase into commercial cultivars could create transgenic citrus varieties producing fruits potentially free of limonoid bitterness