共查询到20条相似文献,搜索用时 15 毫秒
1.
Verónica Beatriz Rajal Alicia Graciela Cid Guillermo Ellenrieder Carlos Mario Cuevas 《World journal of microbiology & biotechnology》2009,25(6):1025-1033
Penicillium ulaiense is a post-harvest pathogenic fungus that attacks citrus fruits. The objective of this work was to study this microorganism
as an α-l-rhamnosidase producer and to characterize it from P. ulaiense. The enzyme under study is used for different applications in food and beverage industries. α-l-Rhamnosidase was produced in a stirred-batch reactor using rhamnose as the main carbon source. The kinetic parameters for
the growth of the fungi and for the enzyme production were calculated from the experimental values. A method for partial purification,
including (NH4)2SO4 precipitation, incubation at pH 12 and DEAE-sepharose chromatography yielded an enzyme with very low β-glucosidase activity.
The pH and temperature optima were 5.0 and 60°C, respectively. The Michaelis–Menten constants for the hydrolysis of p-nitrophenyl-α-l-rhamnoside were V
max = 26 ± 4 IU ml−1 and K
m
= 11 ± 2 mM. The enzyme showed good thermostability up to 60°C and good operational stability in white wine. Co2+ affected positively the activity; EDTA, Mn2+, Mg2+, dithiotreitol and Cu2+ reduced the activity by different amounts, and Hg2+ completely inhibited the enzyme. The enzyme showed more activity on p-nitrophenyl-α-l-rhamnoside than on naringin. According to these results, this enzyme has potential for use in the food and pharmacy industries
since P. ulaiense does not produce mycotoxins. 相似文献
2.
Flax seed mucilage (FM) contains a mixture of highly doubly substituted arabinoxylan as well as rhamnogalacturonan I with
unusual side group substitutions. Treatment of FM with a GH11 Bacillus subtilis XynA endo 1,4-β-xylanase (BsX) gave limited formation of reducing ends but when BsX and FM were incubated together on different
wheat arabinoxylan substrates and birchwood xylan, significant amounts of xylose were released. Moreover, arabinose was released
from both water-extractable and water-unextractable wheat arabinoxylan. Since no xylose or arabinose was released by BsX addition
alone on these substrates, nor without FM or BsX addition, the results indicate the presence of endogenous β-d-xylosidase and α-l-arabinofuranosidase activities in FM. FM also exhibited activity on both p-nitrophenyl α-l-arabinofuranoside (pNPA) and p-nitrophenyl β-d-xylopyranoside (pNPX). Based on K
M
values, the FM enzyme activities had a higher affinity for pNPX (K
M
2 mM) than for pNPA (K
M
20 mM). 相似文献
3.
de Wet BJ Matthew MK Storbeck KH van Zyl WH Prior BA 《Applied microbiology and biotechnology》2008,77(5):975-983
A glycosyl hydrolase family 54 (GH54) α-l-arabinofuranosidase gene (abfA) of Aureobasidium pullulans was amplified by polymerase chain reaction from genomic DNA and a 498-amino-acid open reading frame deduced from the DNA
sequence. Modeling of the highly conserved A. pullulans AbfA protein sequence on the crystal structure of Aspergillus kawachii AkabfB showed that the catalytic amino acid arrangement and overall structure were highly similar including the N-terminal
catalytic and C-terminal arabinose binding domains. The abfA gene was expressed in Saccharomyces cerevisiae, and the heterologous enzyme was purified. The protein was monomeric, migrating at 49 kDa on sodium dodecyl sulfate-polyacrylamide
gel electrophoresis and eluting at 36 kDa upon gel filtration. AbfA showed maximal activity at 55°C and between pH 3.5 and
pH 4. The enzyme had a K
m value for p-nitrophenyl-α-l-arabinofuranoside of 3.7 mM and a V
max of 34.8 μmol min−1 mg protein−1. Arabinose acted as a noncompetitive inhibitor with a K
i of 38.4 mM. The enzyme released arabinose from maize fiber, oat spelt arabinoxylan, and wheat arabinoxylan, but not from
larch wood arabinogalactan or α-1,5-debranched arabinan. AbfA displayed low activity against α-1,5-l-arabino-oligosaccharides. The enzyme acted synergistically with endo-β-1,4-xylanase in the breakdown of wheat arabinoxylan. Binding of AbfA to xylan from several sources confirmed the presence
of a functional carbohydrate-binding module.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. 相似文献
4.
Camila Ramos dos Santos Fábio Márcio Squina Andréia Meza Navarro Daiane Patrícia Oldiges Adriana Franco Paes Leme Roberto Ruller Andrew John Mort Rolf Prade Mário Tyago Murakami 《Biotechnology letters》2011,33(1):131-137
A hyperthermostable glycoside hydrolase family 51 (GH51) α-l-arabinofuranosidase from Thermotoga petrophila RKU-1 (TpAraF) was cloned, overexpressed, purified and characterized. The recombinant enzyme had optimum activity at pH 6.0
and 70°C with linear α-1,5-linked arabinoheptaose as substrate. The substrate cleavage pattern monitored by capillary zone
electrophoresis showed that TpAraF is a classical exo-acting enzyme producing arabinose as its end-product. Far-UV circular
dichroism analysis displayed a typical spectrum of α/β barrel proteins analogously observed for other GH51 α-l-arabinofuranosidases. Moreover, TpAraF was crystallized in two crystalline forms, which can be used to determine its crystallographic
structure. 相似文献
5.
Sakamoto T Ogura A Inui M Tokuda S Hosokawa S Ihara H Kasai N 《Applied microbiology and biotechnology》2011,90(1):137-146
6.
Canakci S Belduz AO Saha BC Yasar A Ayaz FA Yayli N 《Applied microbiology and biotechnology》2007,75(4):813-820
The gene encoding an α-l-arabinofuranosidase from Geobacillus caldoxylolyticus TK4, AbfATK4, was isolated, cloned, and sequenced. The deduced protein had a molecular mass of about 58 kDa, and analysis
of its amino acid sequence revealed significant homology and conservation of different catalytic residues with α-l-arabinofuranosidases belonging to family 51 of the glycoside hydrolases. A histidine tag was introduced at the N-terminal
end of AbfATK4, and the recombinant protein was expressed in Escherichia coli BL21, under control of isopropyl-β-D-thiogalactopyranoside-inducible T7 promoter. The enzyme was purified by nickel affinity
chromatography. The molecular mass of the native protein, as determined by gel filtration, was about 236 kDa, suggesting a
homotetrameric structure. AbfATK4 was active at a broad pH range (pH 5.0–10.0) and at a broad temperature range (40–85°C),
and it had an optimum pH of 6.0 and an optimum temperature of 75–80°C. The enzyme was more thermostable than previously described
arabinofuranosidases and did not lose any activity after 48 h incubation at 70°C. The protein exhibited a high level of activity
with p-nitrophenyl-α-l-arabinofuranoside, with apparent K
m and V
max values of 0.17 mM and 588.2 U/mg, respectively. AbfATK4 also exhibited a low level of activity with p-nitrophenyl-β-d-xylopyranoside, with apparent K
m and V
max values of 1.57 mM and 151.5 U/mg, respectively. AbfATK4 released l-arabinose only from arabinan and arabinooligosaccharides. No endoarabinanase activity was detected. These findings suggest
that AbfATK4 is an exo-acting enzyme. 相似文献
7.
Rojas NL Voget CE Hours RA Cavalitto SF 《Journal of industrial microbiology & biotechnology》2011,38(9):1515-1522
Rhamnosidases are enzymes that catalyze the hydrolysis of terminal nonreducing L-rhamnose for the bioconversion of natural or synthetic rhamnosides. They are of great significance in the current biotechnological
area, with applications in food and pharmaceutical industrial processes. In this study we isolated and characterized a novel
alkaline rhamnosidase from Acrostalagmus luteo albus, an alkali-tolerant soil fungus from Argentina. We also present an efficient, simple, and inexpensive method for purifying
the A. luteo albus rhamnosidase and describe the characteristics of the purified enzyme. In the presence of rhamnose as the sole carbon source,
this fungus produces a rhamnosidase with a molecular weight of 109 kDa and a pI value of 4.6, as determined by SDS–PAGE and
analytical isoelectric focusing, respectively. This enzyme was purified to homogeneity by chromatographic and electrophoretic
techniques. Using p-nitrofenil-α-L-rhamnopiranoside as substrate, the enzyme activity showed pH and temperature optima of 8.0 and 55°C, respectively. The enzyme
exhibited Michaelis–Menten kinetics, with K
M and V
max values of 3.38 mmol l−1 and 68.5 mmol l−1 min−1, respectively. Neither divalent cations such as Ca2+, Mg2+, Mn2+, and Co2+ nor reducing agents such as β-mercaptoethanol and dithiothreitol showed any effect on enzyme activity, whereas this activity
was completely inhibited by Zn2+ at a concentration of 0.2 mM. This enzyme showed the capacity to hydrolyze some natural rhamnoglucosides such as hesperidin,
naringin and quercitrin under alkaline conditions. Based on these results, and mainly due to the high activity of the A. luteo albus rhamnosidase under alkaline conditions, this enzyme should be considered a potential new biocatalyst for industrial applications. 相似文献
8.
Cobucci-Ponzano B Conte F Rossi M Moracci M 《Extremophiles : life under extreme conditions》2008,12(1):61-68
Glycoside hydrolases form hyperthermophilic archaea are interesting model systems for the study of catalysis at high temperatures
and, at the moment, their detailed enzymological characterization is the only approach to define their role in vivo. Family
29 of glycoside hydrolases classification groups α-l-fucosidases involved in a variety of biological events in Bacteria and Eukarya. In Archaea the first α-l-fucosidase was identified in Sulfolobus solfataricus as interrupted gene expressed by programmed −1 frameshifting. In this review, we describe the identification of the catalytic
residues of the archaeal enzyme, by means of the chemical rescue strategy. The intrinsic stability of the hyperthermophilic
enzyme allowed the use of this method, which resulted of general applicability for β and α glycoside hydrolases. In addition,
the presence in the active site of the archaeal enzyme of a triad of catalytic residues is a rather uncommon feature among
the glycoside hydrolases and suggested that in family 29 slightly different catalytic machineries coexist. 相似文献
9.
Amore A Amoresano A Birolo L Henrissat B Leo G Palmese A Faraco V 《Applied microbiology and biotechnology》2012,94(4):995-1006
An α-l-arabinofuranosidase produced by Pleurotus ostreatus (PoAbf) during solid state fermentation on tomato pomace was identified and the corresponding gene and cDNA were cloned and
sequenced. Molecular analysis showed that the poabf gene carries 26 exons interrupted by 25 introns and has an open reading frame encoding a protein of 646 amino acid residues,
including a signal peptide of 20 amino acid residues. The amino acid sequence similar to the other α-l-arabinofuranosidases indicated that the enzyme encoded by poabf can be classified as a family 51 glycoside hydrolase. Heterologous recombinant expression of PoAbf was carried out in the
yeasts Pichia pastoris and Kluyveromyces lactis achieving the highest production level of the secreted enzyme (180 mg L−1) in the former host. rPoAbf produced in P. pastoris was purified and characterized. It is a glycosylated monomer with a molecular weight of 81,500 Da in denaturing conditions.
Mass spectral analyses led to the localization of a single O-glycosylation site at the level of Ser160. The enzyme is highly specific for α-l-arabinofuranosyl linkages and when assayed with p-nitrophenyl α-l-arabinofuranoside it follows Michaelis–Menten kinetics with a K
M of 0.64 mM and a k
cat of 3,010 min−1. The optimum pH is 5 and the optimal temperature 40°C. It is worth noting that the enzyme shows a very high stability in
a broad range of pH. The more durable activity showed by rPoAbf in comparison to the other α-l-arabinofuranosidases enhances its potential for biotechnological applications and increases interest in elucidating the molecular
bases of its peculiar properties. 相似文献
10.
Soria F Ellenrieder G Oliveira GB Cabrera M Carvalho LB 《Applied microbiology and biotechnology》2012,93(3):1127-1134
α-l-Rhamnosidase from Aspergillus terreus was covalently immobilized on the following ferromagnetic supports: polyethylene terephthalate (Dacron-hydrazide), polysiloxane/polyvinyl
alcohol (POS/PVA), and chitosan. The powdered supports were magnetized by thermal coprecipitation method using ferric and
ferrous chlorides, and the immobilization was carried out via glutaraldehyde. The activity of the Dacron-hydrazide (0.53 nkat/μg
of protein) and POS/PVA (0.59 nkat/μg of protein) immobilized enzyme was significantly higher than that found for the chitosan
derivative (0.06 nkat/μg of protein). The activity–pH and activity–temperature profiles for all immobilized enzymes did not
show difference compared to the free enzyme, except the chitosan derivative that presented higher maximum temperature at 65 °C.
The Dacron-hydrazide derivative thermal stability showed a similar behavior of the free enzyme in the temperature range of
40–70 °C. The POS/PVA and chitosan derivatives were stable up to 60 °C, but were completely inactivated at 70 °C. The activity
of the preparations did not appreciably decrease after ten successive reuses. Apparent K
m of α-l-rhamnosidase immobilized on magnetized Dacron-hydrazide (1.05 ± 0.22 mM), POS/PVA (0.57 ± 0.09 mM), and chitosan (1.78 ± 0.24 mM)
were higher than that estimated for the soluble enzyme (0.30 ± 0.03 mM). The Dacron-hydrazide enzyme derivative showed better
performance than the free enzyme to hydrolyze 0.3% narigin (91% and 73% after 1 h, respectively) and synthesize rhamnosides
(0.116 and 0.014 mg narirutin after 1 h, respectively). 相似文献
11.
l-β-Haloalanines are physiologically active unnatural amino acids and they are useful intermediates for the synthesis of natural
and unnatural amino acids, S-linked glycopeptides, and lanthionines. In general l-β-haloalanines were prepared predominantly from l-serine via functional group transformation. Here we reported an alternative approach for the preparation of l-β-haloalanines via halogenation of protected l-cysteine esters which was obtained from l-cysteine or l-cystine, respectively. The mercapto group of protected l-cysteine esters was efficiently transformed to halo groups by triphenylphosphine/N-halosuccinimides. It has been proved to be a versatile desulfurization strategy via this functional group transformation. 相似文献
12.
β-N-Methylamino-l-alanine (BMAA), a non-proteinogenic amino acid, has been detected in a range of cyanobacteria, including terrestrial, aquatic,
free living and endosymbiotic species. The widespread occurrence of cyanobacteria in the environment raises concerns regarding
the ecological and toxicological impact of BMAA, and consequently, studies have focussed extensively on the toxicity and environmental
impact of BMAA, while no research has addressed the ecophysiological or metabolic role of the compound in cyanobacteria. In
this study, both the uptake of exogenous BMAA by and the effect of exogenous BMAA on the growth of Synechocystis PCC6803 were investigated. BMAA was rapidly taken up by the non-diazotrophic cyanobacterium Synechocystis PCC6803 in a concentration dependent manner. The presence of exogenous BMAA resulted in a substantial and concentration-dependent
decrease in cell growth and the substantial loss of photosynthetic pigmentation. Similar effects were seen in the presence
of the non-proteinogenic amino acid, 2,4-diaminobutyric acid but to a lesser degree than that of BMAA. The effects were reversed
when light was decreased from 16 to 10 μmol m−2 s−1. Control cultures grown in the presence of l-arginine, l-asparagine, l-glutamate and glycine showed normal or slightly increased growth with no change in pigmentation. The decrease in growth rate
coupled to bleaching indicates that BMAA may induce chlorosis in the presence of adequate photosynthetic radiation suggesting
a connection between BMAA and the induction of conditions, such as nitrogen or sulphur depletion, that result in growth arrest
and the induction of chlorosis. 相似文献
13.
A set of filamentous fungi (42 strains) was screened for alpha-N-acetylgalactosaminidase activity, and a series of inducers and different cultivation conditions were tested. Enzyme production by the best producer Aspergillus niger CCIM K2 was optimized and scaled up. alpha-N-Acetylgalactosaminidase was purified to apparent homogeneity by cation exchange chromatography, gel filtration, and chromatofocusing, and basic biochemical data of the enzyme were determined: The native molecular weight was estimated by gel filtration to be approximately 440 kDa, the molecular weight of the subunit was determined to be 76 kDa and the pI = 4.8. The K (M) was 0.73 mmol/l for o-nitrophenyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside (o-NP-alpha-GalNAc), and optimum enzyme activity was achieved at pH 1.8 and 55 degrees C. This alpha-N-acetylgalactosaminidase is a retaining-type glycosidase, and it was N-deglycosylated without any loss of activity. 相似文献
14.
A bacterial strain, MAK-2, was isolated as a producer of α-l-rhamnosidase from a soil sample of Dehradoon, India. The strain was identified based on morphology, physiological tests and
16S rDNA analysis. The phylogenetic analysis based on the 16S rDNA sequence, identified the isolate as Staphylococcus xylosus, a non-pathogenic member of CNS (coagulase-negative staphylococci) family. The strain was capable of producing α-l-rhamnosidase by hydrolysing flavonoids thus confirming potential application in the citrus-processing industry. 相似文献
15.
Kapil Tahlan Marcus A. Moore Susan E. Jensen 《Journal of industrial microbiology & biotechnology》2017,44(4-5):517-524
The δ-(l-α-aminoadipyl)-l-cysteinyl-d-valine (ACV) tripeptide is the first dedicated intermediate in the biosynthetic pathway leading to the penicillin and cephalosporin classes of β-lactam natural products in bacteria and fungi. It is synthesized nonribosomally by the ACV synthetase (ACVS) enzyme, which has been purified and partially characterized from many sources. Due to its large size and instability, many details regarding the reaction mechanism of ACVS are still not fully understood. In this review we discuss the chronology and associated methodology that led to the discovery of ACVS, some of the main findings regarding its activities, and some recent/current studies being conducted on the enzyme. In addition, we conclude with perspectives on what can be done to increase our understating of this very important protein in the future. 相似文献
16.
A lectin present in seeds of Clitoria ternatea agglutinated trypsin-treated human B erythrocytes. The sugar specificity assay indicated that lectin belongs to Gal/Gal NAc-specific
group. Hence the lectin, designated C. ternatea agglutinin (CTA), was purified by the combination of acetic acid precipitation, salt fractionation and affinity chromatography.
HPLC gel filtration, SDS-polyacrylamide gel electrophoresis and mass spectrometry indicated that the native lectin is composed
of two identical subunits of molecular weight 34.7 kDa associated by non covalent bonds. The N-terminal sequence of CTA shared
homology with Glycine max and Pisum sativum. Complete sequence was also found to be homologous to S-64 protein of Glycine max, suggesting that CTA probably exhibits both hemagglutination and probably sugar uptake activity. The carbohydrate binding
specificity of the lectin was investigated by quantitative turbidity measurements, and percent inhibition assays. Based on
these assays, we conclude that CTA binds β-d-galactosides, and also may has an extended specificity towards non-reducing terminal Neu5Acα2,6Gal. 相似文献
17.
Hee-Kyoung Jung Joo-Heon Hong Seung-Chun Park Byung-Kwon Park Doo-Hyun Nam Sang-Dal Kim 《Biotechnology and Bioprocess Engineering》2007,12(6):713-719
This study was conducted to develop a bacterial glucan as an animal feed additive. A novel glucan-producing bacterium.Paenibacillus polymyxa JB115, was isolated from Korean soil. The glucan, JB115-BG, produced byP. polymyxa JB115, was confirmed by TLC to be composed of glucose only. By examining FT-IR,1H NMR, and13C NMR spectra, it was proven that JB115-BG has a β-(1→3)- and β-(1→6)-linked glucan structure. The particle size of JB115-BG
was distributed in the range of 4–800 μm, with a mean value of 149.1 μm, and its molecular distribution ranged from 6.9∼3,103.7
kDa. It was also observed that 80% of the purified JB115-BG had a molecular distribution above 100 kDa. The obtained results
suggest that the glucan JB115-BG can be used as an animal feed additive for the purpose of enhancing immunity. 相似文献
18.
Poly(ε-l-lysine) (ε-PL) is a naturally occurring poly(amino acid) characterized by a unique structure linking ε-amino and carboxyl
groups of l-lysine. Due to its various functions and its biodegradability and non-toxicity, the ε-PL polymer has attracted increasing
attention in recent years. ε-PL is frequently found in various strains of Streptomyces sp. This review gives an up-to-date overview regarding the biosynthesis of ε-PL focussing mainly on results obtained from
ten newly isolated producer strains, using the two-stage culture method of cell growth and ε-PL production cultures. The production
of nearly monodispersed ε-PL is covered together with the development of ε-PL specific hydrolases and the release of synthesized
ε-PL into the culture broth. From these results, coupled with the termination of polymerization through nucleophilic chain
transfer, the biosynthetic mechanism of the polymer is discussed. 相似文献
19.
Zanoelo FF Polizeli Md Mde L Terenzi HF Jorge JA 《Journal of industrial microbiology & biotechnology》2004,31(4):170-176
The thermophilic fungus Scytalidium thermophilum produced large amounts of periplasmic -D-xylosidase activity when grown on xylan as carbon source. The presence of glucose in the fresh culture medium drastically reduced the level of -D-xylosidase activity, while cycloheximide prevented induction of the enzyme by xylan. The mycelial -xylosidase induced by xylan was purified using a procedure that included heating at 50°C, ammonium sulfate fractioning (30–75%), and chromatography on Sephadex G-100 and DEAE-Sephadex A-50. The purified -D-xylosidase is a monomer with an estimated molecular mass of 45 kDa (SDS-PAGE) or 38 kDa (gel filtration). The enzyme is a neutral protein (pI 7.1), with a carbohydrate content of 12% and optima of temperature and pH of 60°C and 5.0, respectively. -D-Xylosidase activity is strongly stimulated and protected against heat inactivation by calcium ions. In the absence of substrate, the enzyme is stable for 1 h at 60°C and has half-lives of 11 and 30 min at 65°C in the absence or presence of calcium, respectively. The purified -D-xylosidase hydrolyzed p-nitrophenol--D-xylopyranoside and p-nitrophenol--D-glucopyranoside, exhibiting apparent Km and Vmax values of 1.3 mM, 88 mol min–1 protein–1 and 0.5 mM, 20 mol min–1 protein–1, respectively. The purified enzyme hydrolyzed xylobiose, xylotriose, and xylotetraose, and is therefore a true -D-xylosidase. Enzyme activity was completely insensitive to xylose, which inhibits most -xylosidases, at concentrations up to 200 mM. Its thermal stability and high xylose tolerance qualify this enzyme for industrial applications. The high tolerance of S. thermophilum -xylosidase to xylose inhibition is a positive characteristic that distinguishes this enzyme from all others described in the literature. 相似文献
20.
Lesław B. Lahuta Joanna Goszczyńska Marcin Horbowicz Czesław Hołdyński Ryszard J. Górecki 《Acta Physiologiae Plantarum》2010,32(5):933-942
The mechanism preferentially regulating accumulation of raffinose family oligosaccharides (RFOs) or galactosyl cyclitols in
legume seeds still remains unknown. The broad range of raffinose family oligosaccharides and galactosyl pinitols in the composition
of seeds of Vicia genus gives researchers an exceptional opportunity for investigations on relationships in biosynthesis of both types of α-d-galactosides. Feeding explants of Vicia species radically different in the composition of RFOs and galactosyl pinitols with basic galactose acceptors, sucrose (for
RFOs) or cyclitols (for galactosyl cyclitols) can be a helpful method for assessment of their regulatory role in accumulation
of α-d-galactosides in seeds. Garden vetch (Vicia sativa L.) seeds, naturally accumulating RFOs, demonstrated an ability to take up and use exogenously applied d-pinitol and d-chiro-inositol for synthesis of their mono-, di- and tri-galactosides. Together with the accumulation of new galactosides, the
concentration of RFOs decreased. In fine-leaved (Vicia tenuifolia Roth.) vetch seeds such a remarkably high concentration of galactosyl pinitols (GPs) was discovered that they nearly replaced
RFOs, which is unique among legumes. If the accumulation of both types of galactosides is correlated with concentration of
galactose acceptors, elevated levels of sucrose or myo-inositol should promote accumulation of RFOs, instead of GPs. Unexpectedly, feeding fine-leaved vetch raceme explants with
myo-inositol or sucrose promoted accumulation of GPs, but not of RFOs. Our comparison of accumulation and biosynthesis of both
types of galactosides (RFOs and GPs) throughout development and maturation of seeds from fine-leaved vetch has indicated that
preferential accumulation of GPs is associated with the drying of seeds during maturation. Different patterns in activities
of enzymes engaged in RFOs’ biosynthetic pathway and galactosyltransferases involved in biosynthesis of GPs indicated that
distinct forms of enzymes can operate in both pathways. The feeding of explants with d-chiro-inositol causes accumulation of fagopyritols B1 in seeds of both Vicia species, which suggests presence of the same or a similar form of galactinol synthase. Accumulation of fagopyritols in fine-leaved
vetch seeds did not affect accumulation of RFOs or galactosyl pinitols. 相似文献