13 results on '"Chiang, Chien-Min"'
Search Results
2. Production of a new triterpenoid disaccharide saponin from sequential glycosylation of ganoderic acid A by 2 Bacillus glycosyltransferases.
- Author
-
Chang TS, Chiang CM, Wu JY, Tsai YL, and Ting HJ
- Subjects
- Chromatography, High Pressure Liquid, Glycosylation, Lanosterol metabolism, Reishi metabolism, Solubility, Bacillus enzymology, Disaccharides biosynthesis, Glycosyltransferases metabolism, Heptanoic Acids metabolism, Lanosterol analogs & derivatives, Saponins biosynthesis, Triterpenes metabolism
- Abstract
Ganoderic acid A (GAA) is a lanostane-type triterpenoid, isolated from medicinal fungus Ganoderma lucidum, and possesses multiple bioactivities. In the present study, GAA was sequentially biotransformed by 2 recently discovered Bacillus glycosyltransferases (GT), BtGT_16345 and BsGT110, and the final product was purified and identified as a new compound, GAA-15,26-O-β-diglucoside, which showed 1024-fold aqueous solubility than GAA., (© The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.)
- Published
- 2021
- Full Text
- View/download PDF
3. Biotransformation of celastrol to a novel, well-soluble, low-toxic and anti-oxidative celastrol-29-O-β-glucoside by Bacillus glycosyltransferases.
- Author
-
Chang TS, Wang TY, Chiang CM, Lin YJ, Chen HL, Wu YW, Ting HJ, and Wu JY
- Subjects
- Animals, Antioxidants toxicity, Bacillus subtilis metabolism, Biotransformation, Glucosides toxicity, Pentacyclic Triterpenes, Solubility, Antioxidants chemistry, Antioxidants metabolism, Bacillus subtilis enzymology, Glucosides chemistry, Glucosides metabolism, Glycosyltransferases metabolism, Triterpenes metabolism
- Abstract
Celastrol is a quinone-methide triterpenoid isolated from the root extracts of Tripterygium wilfordii (Thunder god vine). Although celastrol possesses multiple bioactivities, the potent toxicity and rare solubility in water hinder its clinical application. Biotransformation of celastrol using either whole cells or purified enzymes to form less toxic and more soluble derivatives has been proven difficult due to its potent antibiotic and enzyme-conjugation property. The present study evaluated biotransformation of celastrol by four glycosyltransferases from Bacillus species and found one glycosyltransferase (BsGT110) from Bacillus subtilis with significant activity toward celastrol. The biotransformation metabolite was purified and identified as celastrol-29-O-β-glucoside by mass and nuclear magnetic resonance spectroscopy. Celastrol-29-O-β-glucoside showed over 53-fold higher water solubility than celastrol, while maintained 50% of the free radical scavenging activity of celastrol. When using zebrafish as the in vivo animal model, celastrol-29-O-β-glucoside exhibited 50-fold less toxicity than celastrol. To our knowledge, the present study is not only the first report describing the biotransformation of celastrol, but also the first one detailing a new compound, celastrol-29-O-β-glucoside, that is generated in the biotransformation process. Moreover, celastrol-29-O-β-glucoside may serve as a potential candidate in the future medicine application due to its higher water solubility and lower toxicity., (Copyright © 2020 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.)
- Published
- 2021
- Full Text
- View/download PDF
4. A Genome-Centric Approach Reveals a Novel Glycosyltransferase from the GA A07 Strain of Bacillus thuringiensis Responsible for Catalyzing 15- O -Glycosylation of Ganoderic Acid A.
- Author
-
Chang TS, Wang TY, Hsueh TY, Lee YW, Chuang HM, Cai WX, Wu JY, Chiang CM, and Wu YW
- Subjects
- Bacillus thuringiensis genetics, Bacterial Proteins genetics, Biotransformation, Catalysis, Glycosylation, Glycosyltransferases genetics, Lanosterol chemistry, Lanosterol metabolism, Phylogeny, Substrate Specificity, Whole Genome Sequencing, Bacillus thuringiensis enzymology, Bacterial Proteins metabolism, Genome, Bacterial, Glycosyltransferases metabolism, Heptanoic Acids chemistry, Heptanoic Acids metabolism, Lanosterol analogs & derivatives
- Abstract
Strain GA A07 was identified as an intestinal Bacillus bacterium of zebrafish, which has high efficiency to biotransform the triterpenoid, ganoderic acid A (GAA), into GAA-15- O -β-glucoside. To date, only two known enzymes (BsUGT398 and BsUGT489) of Bacillus subtilis ATCC 6633 strain can biotransform GAA. It is thus worthwhile to identify the responsible genes of strain GA A07 by whole genome sequencing. A complete genome of strain GA A07 was successfully assembled. A phylogenomic analysis revealed the species of the GA A07 strain to be Bacillus thuringiensis . Forty glycosyltransferase (GT) family genes were identified from the complete genome, among which three genes ( FQZ25_16345 , FQZ25_19840 , and FQZ25_19010 ) were closely related to BsUGT398 and BsUGT489. Two of the three candidate genes, FQZ25_16345 and FQZ25_19010 , were successfully cloned and expressed in a soluble form in Escherichia coli , and the corresponding proteins, BtGT_16345 and BtGT_19010, were purified for a biotransformation activity assay. An ultra-performance liquid chromatographic analysis further confirmed that only the purified BtGT_16345 had the key biotransformation activity of catalyzing GAA into GAA-15- O -β-glucoside. The suitable conditions for this enzyme activity were pH 7.5, 10 mM of magnesium ions, and 30 °C. In addition, BtGT_16345 showed glycosylation activity toward seven flavonoids (apigenein, quercetein, naringenein, resveratrol, genistein, daidzein, and 8-hydroxydaidzein) and two triterpenoids (GAA and antcin K). A kinetic study showed that the catalytic efficiency (k
cat /KM ) of BtGT_16345 was not significantly different compared with either BsUGT398 or BsUGT489. In short, this study identified BtGT_16345 from B. thuringiensis GA A07 is the catalytic enzyme responsible for the 15- O -glycosylation of GAA and it was also regioselective toward triterpenoid substrates.- Published
- 2019
- Full Text
- View/download PDF
5. A New Triterpenoid Glucoside from a Novel Acidic Glycosylation of Ganoderic Acid A via Recombinant Glycosyltransferase of Bacillus subtilis .
- Author
-
Chang TS, Chiang CM, Kao YH, Wu JY, Wu YW, and Wang TY
- Subjects
- Amino Acid Sequence, Biotransformation, Catalysis, Chromatography, High Pressure Liquid, Glucosides chemistry, Glycosylation, Heptanoic Acids chemistry, Kinetics, Lanosterol chemistry, Lanosterol metabolism, Triterpenes chemistry, Bacillus subtilis enzymology, Glucosides biosynthesis, Glycosyltransferases metabolism, Heptanoic Acids metabolism, Lanosterol analogs & derivatives, Recombinant Proteins, Triterpenes metabolism
- Abstract
Ganoderic acid A (GAA) is a bioactive triterpenoid isolated from the medicinal fungus Ganoderma lucidum . Our previous study showed that the Bacillus subtilis ATCC (American type culture collection) 6633 strain could biotransform GAA into compound ( 1 ), GAA-15- O -β-glucoside, and compound ( 2 ). Even though we identified two glycosyltransferases (GT) to catalyze the synthesis of GAA-15- O -β-glucoside, the chemical structure of compound ( 2 ) and its corresponding enzyme remain elusive. In the present study, we identified BsGT110, a GT from the same B. subtilis strain, for the biotransformation of GAA into compound ( 2 ) through acidic glycosylation. BsGT110 showed an optimal glycosylation activity toward GAA at pH 6 but lost most of its activity at pH 8. Through a scaled-up production, compound ( 2 ) was successfully isolated using preparative high-performance liquid chromatography and identified to be a new triterpenoid glucoside (GAA-26- O -β-glucoside) by mass and nuclear magnetic resonance spectroscopy. The results of kinetic experiments showed that the turnover number (k
cat ) of BsGT110 toward GAA at pH 6 (kcat = 11.2 min-1 ) was 3-fold higher than that at pH 7 (kcat = 3.8 min-1 ), indicating that the glycosylation activity of BsGT110 toward GAA was more active at acidic pH 6. In short, we determined that BsGT110 is a unique GT that plays a role in the glycosylation of triterpenoid at the C-26 position under acidic conditions, but loses most of this activity under alkaline ones, suggesting that acidic solutions may enhance the catalytic activity of this and similar types of GTs toward triterpenoids.- Published
- 2019
- Full Text
- View/download PDF
6. Potential Industrial Production of a Well-Soluble, Alkaline-Stable, and Anti-Inflammatory Isoflavone Glucoside from 8-Hydroxydaidzein Glucosylated by Recombinant Amylosucrase of Deinococcus geothermalis .
- Author
-
Chang TS, Wang TY, Yang SY, Kao YH, Wu JY, and Chiang CM
- Subjects
- Anti-Inflammatory Agents chemistry, Anti-Inflammatory Agents pharmacology, Biotransformation, Drug Stability, Fermentation, Genetic Vectors, Glucosides chemistry, Glucosides pharmacology, Isoflavones chemistry, Isoflavones metabolism, Isoflavones pharmacology, Molecular Structure, Recombinant Proteins biosynthesis, Recombinant Proteins genetics, Solubility, Anti-Inflammatory Agents metabolism, Deinococcus genetics, Deinococcus metabolism, Glucosides biosynthesis, Glucosyltransferases genetics, Glucosyltransferases metabolism, Isoflavones biosynthesis
- Abstract
8-Hydroxydaidzein (8-OHDe), an ortho -hydroxylation derivative of soy isoflavone daidzein isolated from some fermented soybean foods, has been demonstrated to possess potent anti-inflammatory activity. However, the isoflavone aglycone is poorly soluble and unstable in alkaline solutions. To improve the aqueous solubility and stability of the functional isoflavone, 8-OHDe was glucosylated with recombinant amylosucrase of Deinococcus geothermalis (DgAS) with industrial sucrose, instead of expensive uridine diphosphate-glucose (UDP-glucose). One major product was produced from the biotransformation, and identified as 8-OHDe-7-α-glucoside, based on mass and nuclear magnetic resonance spectral analyses. The aqueous solubility and stability of the isoflavone glucoside were determined, and the results showed that the isoflavone glucoside was almost 4-fold more soluble and more than six-fold higher alkaline-stable than 8-OHDe. In addition, the anti-inflammatory activity of 8-OHDe-7-α-glucoside was also determined by the inhibition of lipopolysaccharide-induced nitric oxide production in RAW 264.7 cells. The results showed that 8-OHDe-7-α-glucoside exhibited significant and dose-dependent inhibition on the production of nitric oxide, with an IC
50 value of 173.2 µM, which remained 20% of the anti-inflammatory activity of 8-OHDe. In conclusion, the well-soluble and alkaline-stable 8-OHDe-7-α-glucoside produced by recombinant DgAS with a cheap substrate, sucrose, as a sugar donor retains moderate anti-inflammatory activity, and could be used in industrial applications in the future.- Published
- 2019
- Full Text
- View/download PDF
7. Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15- O -Glycosylation of Ganoderic Acid A.
- Author
-
Chang TS, Wu JY, Wang TY, Wu KY, and Chiang CM
- Subjects
- Biotransformation, Glycosylation, Heptanoic Acids chemistry, Hydrogen-Ion Concentration, Ions, Lanosterol chemistry, Lanosterol metabolism, Metals pharmacology, Phylogeny, Temperature, Bacillus subtilis enzymology, Biocatalysis, Glycosyltransferases metabolism, Heptanoic Acids metabolism, Lanosterol analogs & derivatives, Uridine Diphosphate metabolism
- Abstract
Bacillus subtilis ATCC (American type culture collection) 6633 was found to biotransform ganoderic acid A (GAA), which is a major lanostane triterpenoid from the medicinal fungus Ganoderma lucidum . Five glycosyltransferase family 1 (GT1) genes of this bacterium, including two uridine diphosphate-dependent glycosyltransferase (UGT) genes, BsUGT398 and BsUGT489 , were cloned and overexpressed in Escherichia coli . Ultra-performance liquid chromatography confirmed the two purified UGT proteins biotransform ganoderic acid A into a metabolite, while the other three purified GT1 proteins cannot biotransform GAA. The optimal enzyme activities of BsUGT398 and BsUGT489 were at pH 8.0 with 10 mM of magnesium or calcium ion. In addition, no candidates showed biotransformation activity toward antcin K, which is a major ergostane triterpenoid from the fruiting bodies of Antrodia cinnamomea . One biotransformed metabolite from each BsUGT enzyme was then isolated with preparative high-performance liquid chromatography. The isolated metabolite from each BsUGT was identified as ganoderic acid A-15- O -β-glucoside by mass and nuclear magnetic resonance spectroscopy. The two BsUGTs in the present study are the first identified enzymes that catalyze the 15- O -glycosylation of triterpenoids.
- Published
- 2018
- Full Text
- View/download PDF
8. New Triterpenoid from Novel Triterpenoid 15- O -Glycosylation on Ganoderic Acid A by Intestinal Bacteria of Zebrafish.
- Author
-
Chang TS, Chiang CM, Wang TY, Lee CH, Lee YW, and Wu JY
- Subjects
- Animals, Bacillus classification, Bacillus genetics, Bacillus isolation & purification, Bacillus metabolism, Bacteria genetics, Bacteria isolation & purification, Bacteria metabolism, Catalysis, Chromatography, High Pressure Liquid, Gastrointestinal Microbiome, Glycosylation, Phylogeny, RNA, Ribosomal, 16S genetics, Bacteria classification, Triterpenes chemistry, Zebrafish microbiology
- Abstract
Functional bacteria that could biotransform triterpenoids may exist in the diverse microflora of fish intestines. Ganoderic acid A (GAA) is a major triterpenoid from the medicinal fungus Ganoderma lucidum . In studying the microbial biotransformation of GAA, dozens of intestinal bacteria were isolated from the excreta of zebrafish. The bacteria's ability to catalyze GAA were determined using ultra-performance liquid chromatography analysis. One positive strain, GA A07, was selected for functional studies. GA A07 was confirmed as Bacillus sp., based on the DNA sequences of the 16S rRNA gene. The biotransformed metabolite was purified with the preparative high-performance liquid chromatography method and identified as GAA-15- O -β-glucoside, based on the mass and nuclear magnetic resonance spectral data. The present study is the first to report the glycosylation of Ganoderma triterpenoids. Moreover, 15- O -glycosylation is a new microbial biotransformation of triterpenoids, and the biotransformed metabolite, GAA-15- O -β-glucoside, is a new compound.
- Published
- 2018
- Full Text
- View/download PDF
9. Production and Anti-Melanoma Activity of Methoxyisoflavones from the Biotransformation of Genistein by Two Recombinant Escherichia coli Strains.
- Author
-
Chiang CM, Chang YJ, Wu JY, and Chang TS
- Subjects
- Animals, Antineoplastic Agents, Phytogenic isolation & purification, Antineoplastic Agents, Phytogenic pharmacology, Bacillus megaterium chemistry, Bacillus megaterium enzymology, Bacterial Proteins genetics, Biotransformation, Cell Line, Tumor, Cell Survival drug effects, Escherichia coli chemistry, Escherichia coli genetics, Fibroblasts drug effects, Genistein metabolism, Hydroxylation, Inhibitory Concentration 50, Isoflavones isolation & purification, Isoflavones pharmacology, Melanoma, Experimental pathology, Metabolic Engineering methods, Methylation, Methyltransferases genetics, Mice, Monophenol Monooxygenase genetics, Organ Specificity, Organisms, Genetically Modified genetics, Organisms, Genetically Modified metabolism, Streptomyces chemistry, Streptomyces enzymology, Transgenes, Antineoplastic Agents, Phytogenic biosynthesis, Bacterial Proteins metabolism, Escherichia coli metabolism, Isoflavones biosynthesis, Methyltransferases metabolism, Monophenol Monooxygenase metabolism
- Abstract
Biotransformation of the soy isoflavone genistein by sequential 3'-hydroxylation using recombinant Escherichia coli expressing tyrosinase from Bacillus megaterium and then methylation using another recombinant E. coli expressing O -methyltransferase from Streptomyces peucetius was conducted. The results showed that two metabolites were produced from the biotransformation, identified as 5,7,4'-trihydroxy-3'-methoxyisoflavone and 5,7,3'-trihydroxy-4'-methoxyisoflavone, respectively, based on their mass and nuclear magnetic resonance spectral data. 5,7,4'-Trihydroxy-3'-methoxyisoflavone showed potent antiproliferative activity toward mouse B16 melanoma cells with an IC
50 value of 68.8 μM. In contrast, the compound did not show any cytotoxicity toward mouse normal fibroblast cells, even at 350 μM concentration. The results of the present study offer insight on the production of both 5,7,4'-trihydroxy-3'-methoxyisoflavone and 5,7,3'-trihydroxy-4'-methoxyisoflavone by two recombinant E. coli strains and the potential anti-melanoma applications of 5,7,4'-trihydroxy-3'-methoxyisoflavone.- Published
- 2017
- Full Text
- View/download PDF
10. Improving Free Radical Scavenging Activity of Soy Isoflavone Glycosides Daidzin and Genistin by 3'-Hydroxylation Using Recombinant Escherichia coli.
- Author
-
Chiang CM, Wang DS, and Chang TS
- Subjects
- Antioxidants metabolism, Bacillus megaterium enzymology, Biotransformation physiology, Biphenyl Compounds chemistry, Escherichia coli genetics, Glycosides metabolism, Picrates chemistry, Glycine max metabolism, Antioxidants chemistry, Escherichia coli metabolism, Isoflavones chemistry, Isoflavones metabolism, Monophenol Monooxygenase metabolism
- Abstract
The present study describes the biotransformation of a commercially available crude extract of soy isoflavones, which contained significant amounts of the soy isoflavone glycosides daidzin and genistin, by recombinant Escherichia coli expressing tyrosinase from Bacillus megaterium . Two major products were isolated from the biotransformation and identified as 3'-hydroxydaidzin and 3'-hydroxygenistin, respectively, based on their mass and nuclear magnetic resonance spectral data. The two 3'-hydroxyisoflavone glycosides showed potent 2,2-diphenyl-1-picrylhydrazyl free radical scavenging activity with IC
50 values of 7.4 and 9.8 μM for 3'-hydroxydaidzin and 3'-hydroxygenistin, respectively. The free radical scavenging activities of the two 3'-hydroxyisoflavone glycosides were, respectively, 120 and 72 times higher than the activity of their precursors, daidzin and genistin, and were also stronger than the activity of ascorbic acid, which showed an IC50 value of 15.1 μM. This is the first report of the bio-production and potential antioxidant applications of both 3'-hydroxydaidzin and 3'-hydroxygenistin.- Published
- 2016
- Full Text
- View/download PDF
11. Production of Two Novel Methoxy-Isoflavones from Biotransformation of 8-Hydroxydaidzein by Recombinant Escherichia coli Expressing O-Methyltransferase SpOMT2884 from Streptomyces peucetius.
- Author
-
Chiang CM, Ding HY, Tsai YT, and Chang TS
- Subjects
- Animals, Cell Survival drug effects, Chromatography, High Pressure Liquid, Fermentation, Gene Expression, Isoflavones chemistry, Isoflavones metabolism, Isoflavones pharmacology, Melanoma, Experimental, Mice, Streptomyces enzymology, Biotransformation, Escherichia coli genetics, Escherichia coli metabolism, Isoflavones biosynthesis, Methyltransferases genetics, Methyltransferases metabolism, Streptomyces genetics
- Abstract
Biotransformation of 8-hydroxydaidzein by recombinant Escherichia coli expressing O-methyltransferase (OMT) SpOMT2884 from Streptomyces peucetius was investigated. Two metabolites were isolated and identified as 7,4'-dihydroxy-8-methoxy-isoflavone (1) and 8,4'-dihydroxy-7-methoxy-isoflavone (2), based on mass, 1H-nuclear magnetic resonance (NMR) and 13C-NMR spectrophotometric analysis. The maximum production yields of compound (1) and (2) in a 5-L fermenter were 9.3 mg/L and 6.0 mg/L, respectively. The two methoxy-isoflavones showed dose-dependent inhibitory effects on melanogenesis in cultured B16 melanoma cells under non-toxic conditions. Among the effects, compound (1) decreased melanogenesis to 63.5% of the control at 25 μM. This is the first report on the 8-O-methylation activity of OMT toward isoflavones. In addition, the present study also first identified compound (1) with potent melanogenesis inhibitory activity.
- Published
- 2015
- Full Text
- View/download PDF
12. Inhibitory effect of a water extract from Pemphis acidula on melanogenesis in mouse B16 melanoma cells.
- Author
-
Ding HY, Chang TS, Chiang CM, and Shou-Ku Tai S
- Subjects
- Animals, Cell Line, Tumor, Cell Survival drug effects, Gene Expression Regulation, Enzymologic, Melanins metabolism, Mice, Monophenol Monooxygenase antagonists & inhibitors, Monophenol Monooxygenase metabolism, Plant Bark chemistry, RNA, Messenger genetics, RNA, Messenger metabolism, Lythraceae chemistry, Plant Extracts chemistry, Plant Extracts pharmacology, Water chemistry
- Abstract
The inhibitory effect of a water extract from Pemphis acidula on melanogenesis in mouse B16 melanoma cells was investigated. The results showed that the P. acidula extract (PAE) inhibited melanogenesis in 3-isobutyl-1-methylxanthin (IBMX)-stimulated B16 cells in a dose-dependent manner, with an IC50 value of 33.5 μg/ml. In addition, PAE also inhibited cellular tyrosinase activity. Moreover, western blot and real-time reverse transcriptase polymerase chain reaction (qRT-PCR) analyses respectively confirmed that PAE down-regulated levels of tyrosinase protein and its mRNA in IBMX-stimulated B16 cells. These results demonstrated that PAE inhibits melanogenesis of B16 cells by reducing tyrosinase gene expression. From the present study, PAE is proven to be a good candidate as a skin-whitening agent for treatment of skin hyperpigmentation.
- Published
- 2011
13. Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis.
- Author
-
Chuankhayan P, Hsieh CY, Huang YC, Hsieh YY, Guan HH, Hsieh YC, Tien YC, Chen CD, Chiang CM, and Chen CJ
- Subjects
- Amino Acid Sequence, Crystallography, X-Ray, Enzyme Inhibitors metabolism, Enzyme Inhibitors pharmacology, Glucose metabolism, Glucose pharmacology, Glycoside Hydrolases chemistry, Glycoside Hydrolases metabolism, Hexosyltransferases antagonists & inhibitors, Models, Molecular, Molecular Sequence Data, Structure-Activity Relationship, Aspergillus enzymology, Biocatalysis, Catalytic Domain, Hexosyltransferases chemistry, Hexosyltransferases metabolism
- Abstract
Fructosyltransferases catalyze the transfer of a fructose unit from one sucrose/fructan to another and are engaged in the production of fructooligosaccharide/fructan. The enzymes belong to the glycoside hydrolase family 32 (GH32) with a retaining catalytic mechanism. Here we describe the crystal structures of recombinant fructosyltransferase (AjFT) from Aspergillus japonicus CB05 and its mutant D191A complexes with various donor/acceptor substrates, including sucrose, 1-kestose, nystose, and raffinose. This is the first structure of fructosyltransferase of the GH32 with a high transfructosylation activity. The structure of AjFT comprises two domains with an N-terminal catalytic domain containing a five-blade beta-propeller fold linked to a C-terminal beta-sandwich domain. Structures of various mutant AjFT-substrate complexes reveal complete four substrate-binding subsites (-1 to +3) in the catalytic pocket with shapes and characters distinct from those of clan GH-J enzymes. Residues Asp-60, Asp-191, and Glu-292 that are proposed for nucleophile, transition-state stabilizer, and general acid/base catalyst, respectively, govern the binding of the terminal fructose at the -1 subsite and the catalytic reaction. Mutants D60A, D191A, and E292A completely lost their activities. Residues Ile-143, Arg-190, Glu-292, Glu-318, and His-332 combine the hydrophobic Phe-118 and Tyr-369 to define the +1 subsite for its preference of fructosyl and glucosyl moieties. Ile-143 and Gln-327 define the +2 subsite for raffinose, whereas Tyr-404 and Glu-405 define the +2 and +3 subsites for inulin-type substrates with higher structural flexibilities. Structural geometries of 1-kestose, nystose and raffinose are different from previous data. All results shed light on the catalytic mechanism and substrate recognition of AjFT and other clan GH-J fructosyltransferases.
- Published
- 2010
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.