Synergistic interactions between the genetically modified bacterial polysaccharide P2 and carob or konjac mannan

Rheological studies have confirmed that the bacterial polysaccharide P2, a genetically modified variant of the Acetobacter xylinum polysaccharide acetan, undergoes synergistic gelation with either of the plant polysaccharides carob or konjac mannan. X-ray fibre diffraction data shows that P2 can form a 5-fold helical structure of pitch 4.7nm and an axial rise per disaccharide repeat of 0.92nm. Optical rotation data demonstrate that P2 undergoes a coil-helix transition in solution and that deacylation enhances the stability of the helical structure in solution. Studies made on mixtures prepared at different temperatures and ionic strengths suggest that denaturation of the P2 helix favours interaction and gelation. Deacetylation of P2 enhances gelation. X-ray diffraction data for oriented fibres prepared from deacetylated P2-konjac mannan mixed films reveal a 6-fold helical structure of pitch 5.54nm with an axial rise per disaccharide repeat also of 0.92nm. This mixed helix provides direct evidence for binding between the two polysaccharides. P2 contains two sites of acetylation: one on the backbone and one on the sidechain. The former site of acetylation inhibits helix formation for P2. It is suggested that this site of acetylation also inhibits formation of the mixed helix, explaining the enhanced gelation of mixtures on deacetylation.     

Biosynthesis of papaverine

Tracer experiments have shown that in Papaver somniferum papaverine arises from (−)-norreticuline via norlaudanidine and norlaudanosine.     

Biosynthesis of limonoids in Citrus

Analyses of citrus leaves and fruits, and radioisotope tracer work showed that the leaves could synthesize limonoids and that the trees could translocate limonoids from leaves to the fruit. These results suggest that limonoids in citrus fruit tissues are synthesized in leaves and translocated to the fruit. No evidence was found to support the presence of limonoid biosynthetic systems in the fruit tissues.     

Biosynthesis of piperlongumine

The incorporation of l-[U-¹⁴C]lysine and l-[U-¹⁴C]phenylalanine into piperlongumine has been demonstrated in Piper longum. The subsequent stepwise degradation to methyl-(3,4,5-trimethoxyphenyl)-propanoate and δ-aminovaleric acid revealed that the C₆-C₃ moiety of the alkamide arises from phenylalanine; the heterocyclic ring is biosynthesised from lysine. It has also been shown that dl-[2-¹⁴C]tyrosine and [2-¹⁴C]sodium acetate are poor precursors of piperlongumine.     

Biosynthesis of cannabinoid acids

Malonic acid, mevalonic acid, geraniol and nerol were incorporated into tetrahydrocannabinolic acid and cannabichromenic acid in Cannabis sativa. The pathway from cannabigerolic acid to tetrahydrocannabinolic acid via cannabidiolic acid was established by feeding labelled cannabinoid acids. Cannabichromenic acid was shown to be formed on a side pathway from cannabigerolic acid.     

Arabidopsis thaliana T-DNA Mutants Implicate GAUT Genes in the Biosynthesis of Pectin and Xylan in Cell Walls and Seed Testa

Galacturonosyltransferase 1 （GAUT1） is an α1,4-D-galacturonosyltransferase that transfers galacturonic acid from uridine 5＇-diphosphogalacturonic acid onto the pectic polysaccharide homogalacturonan （Sterling et al., 2006）. The 25-member Arabidopsis thaliana GAUT1-related gene family encodes 15 GAUT and 10 GAUT-like （GATL） proteins with, respectively, 56-84 and 42-53% amino acid sequence similarity to GAUT1. Previous phylogenetic analyses of AtGAUTs indicated three clades： A through C. A comparative phylogenetic analysis of the Arabidopsis, poplar and rice GAUT families has sub-classified the GAUTs into seven clades： clade A-1 （GAUTs 1 to 3）; A-2 （GAUT4）; A-3 （GAUTs 5 and 6）; A-4 （GAUT7）; B-1 （GAUTs 8 and 9）; B-2 （GAUTs 10 and 11）; and clade C （GAUTs 12 to 15）. The Arabidopsis GAUTs have a distribution comparable to the poplar orthologs, with the exception of GAUT2, which is absent in poplar. Rice, however, has no orthologs of GAUTs 2 and 12 and has multiple apparent orthologs of GAUTs 1, 4, and 7 compared with eitherArabidopsis or poplar. The cell wall glycosyl residue compositions of 26 homozygous T-DNA insertion mutants for 13 of 15 Arabidopsis GAUTgenes reveal significantly and reproducibly different cell walls in specific tissues of gaut mutants 6, 8, 9, 10, 11, 12, 13, and 14 from that of wild-type Arabidopsis walls. Pectin and xylan polysaccharides are affected by the loss of GAUT function, as demonstrated by the altered galacturonic acid, xylose, rhamnose, galactose, and arabinose composition of distinct gaut mutant walls. The wall glycosyl residue compositional phenotypes observed among the gaut mutants suggest that at least six different biosynthetic linkages in pectins and/or xylans are affected by the lesions in these GAUTgenes. Evidence is also presented to support a role for GAUT11 in seed mucilage expansion and in seed wall and mucilage composition.     

Characterization of oligosaccharides from an antigenic mannan of Saccharomyces cerevisiae

Mannans of the yeast Saccharomyces cerevisiae have been implicated as containing the allergens to which bakers and brewers are sensitive and also the antigen recognized by patients with Crohn's disease. A fraction of S. cerevisiae mannan, Sc500, having high affinity for antibodies in Crohn's patients has been characterized by NMR spectroscopy followed by fragmentation using alkaline elimination, partial acid hydrolysis and acetolysis. The released oligosaccharides were separated by gel filtration on a Biogel P4 column and analyzed by fluorescence labeling, HPLC and methylation analysis. The relationship between structure and antigen activity was measured by competitive ELISA. The antigenic activity of the original high molecular weight mannan could be ascribed to terminal Man13Man12 sequences which are rarely found in human glycoproteins but were over-represented in Sc500 compared to other yeast mannans.     

Biosynthesis of 3-methoxycarbonylpropylglucosinolate in an Erysimum species

Incorporation of DL-2-aminohexanedioic acid, DL-2-amino-5-methoxycarbonyl-pentanoic acid and DL-methionine into 3-methoxycarbonylpropylglucosinolate have been demonstrated using an Erystmum species. The data support the following sequence of biosynthetic reactions: 2-aminohexanedioic acid is methylated by methionine; the resulting 2-amino-5-methoxycarbonyl-pentanoic acid is then converted into the glucosinolate. 2-Amino-5-methoxycarbonyl-pentanoic acid has been tentatively identified as a natural product in the plant.     

茁霉多糖生物合成的研究进展

本文综述了茁霉多糖的生物合成,简单探讨了其生物合成的机理,并从发酵工艺入手,对通过各种发酵条件的对比,分析并讨论了生物合成的一系列优化结果。同时,简要介绍了茁霉多糖的一些理化性质以及它在工业上的生产应用,并讨论了其应用前景。     

Biosynthesis of gramine in Phalaris arundinacea

The administration of L-tryptophan-[3-¹⁴C] to Phalaris arundinacea L. (Vantage strain) for 9 days resulted in the formation of radioactive gramine (8.2% absolute incorporation). A systematic degradation of the alkaloid indicated that essentially all its activity was located on the methylene group, indicating that its biosynthesis is the same as that occurring in Hordeum species and Lupinus hartwegii.     

Biosynthesis of carvone in Mentha spicata

Degradation of, and measurement of isotope ratios in, (?)-carvone that had been biosynthesized in Mentha spicata from ³H- and ¹⁴C-labelled geraniol and mevalonate indicate that (a) oxidation of limonene or its biogenetic equivalent to form carvone involves shift of the endocyclic double bond; (b) (+)-limonene and (?)-carvone are biogenetically related and are probably formed on divergent pathways from a common intermediate; and (c) the exocyclic double bond of carvone is not formed regiospecifically. These results enable the mechanisms for the introduction of the carbonyl group and for the formation of the isopropenyl side-chain to be delimited.     

Composition of Actinidia mucilage

Purified mucilages extracted from several plant parts of Actinidia chinensis and from the leaves of nine Actinidia species, were shown to be acidic polysaccharides, containing galactose, arabinose, mannose and glucuronic acid. Fucose and xylose were also present in the mucilages from A. chinensis and in the leaf mucilage of four other species. Partial hydrolysis studies suggested that all the mucilages may belong to the glucuronomannan family of polysaccharides, with a repeating disaccharide core of glucuronosylmannose. Division of the Actinidia genus into subgenera may be possible on the basis of properties and monosaccharide compositions of the mucilages.     

Biosynthesis of citreomontanin in Penicillium pedemontanum

The ¹³C NMR spectrum of citreomontanin has been fully assigned by analysis in the presence of a shift reagent. The intramolecular distribution patt     

Biosynthesis of cyanidin in buckwheat hypocotyls

Aminooxyacetate (AOA), an inhibitor of phenylalanine transamination and deamination in vitro, inhibits the light-induced formation of chlorogenic acid, leucoanthocyanin, rutin and anthocyanin (cyanidin glycosides) in buckwheat hypocotyls. Anthocyanin production is inhibited 87 ± 4%, when excised hypocotyls are incubated in 0.5 mM AOA in Petri dishes. AOA is also effective when taken up through the roots or sprayed onto seedlings. In the presence of biosynthetic precursors of cyanidin (l-phenylalanine, trans-cinnamic acid, p-coumaric acid, naringenin, eriodictyol, dihydrokaempferol. and dihydroquercetin) the inhibition of anthocyanin formation caused by AOA is completely or partially reversed. The general applicability of a complementation technique involving AOA or a similar inhibitor of phenylpropane synthesis is proposed to investigate the biosynthesis of natural products derived from cinnamic acid.     

Purification of a β-mannanase enzyme from lucerne seed by substrate affinity chromatography

A technique which employs substrate affinity chromatography on glucomannan- or mannan-AH-Sepharose, has been developed for the purification of legume seed β-mannanases. Using this technique, lucerne seed β-mannanase B has been purified to near homogeneity with a final specific activity of 1080 nkat per mg protein. The preparation was completely devoid of α-galactosidase and β-mannosidase activities. β-Mannanases of microbial origin can also be purified using these materials.