Browse
Submit Data
Databases
API
Help

Dataset Information

21 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Biological upgrading of 3,6-anhydro-L-galactose from agarose to a new platform chemical.

ABSTRACT: Recently, the utilization of renewable biomass instead of fossil fuels for producing fuels and chemicals is receiving much attention due to the global climate change. Among renewable biomass, marine algae are gaining importance as third generation biomass feedstocks owing to their advantages over lignocellulose. Particularly, red macroalgae have higher carbohydrate contents and simpler carbohydrate compositions than other marine algae. In red macroalgal carbphydrates, 3,6-anhydro-L-galactose (AHG) is the main sugar composing agarose along with D-galactose. However, AHG is not a common sugar and is chemically unstable. Thus, not only AHG but also red macroalgal biomass itself cannot be efficiently converted or utilized. Here, we biologically upgraded AHG to a new platform chemical, its sugar alcohol form, 3,6-anhydro-l-galactitol (AHGol), an anhydrohexitol. To accomplish this, we devised an integrated process encompassing a chemical hydrolysis process for producing agarobiose (AB) from agarose and a biological process for converting AB to AHGol using metabolically engineered Saccharomyces cerevisiae to efficiently produce AHGol from agarose with high titers and yields. AHGol was also converted to an intermediate chemical for plastics, isosorbide. To our knowledge, this is the first demonstration of upgrading a red macroalgal biomass component to a platform chemical via a new biological route, by using an engineered microorganism.

SUBMITTER: Kim DH

PROVIDER: S-EPMC8009285 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Similar Datasets

Biocatalytic Conversion of Carrageenans for the Production of 3,6-Anhydro-D-galactose.

Project description:Marine biomass stands out as a sustainable resource for generating value-added chemicals. In particular, anhydrosugars derived from carrageenans exhibit a variety of biological functions, rendering them highly promising for utilization and cascading in food, cosmetic, and biotechnological applications. However, the limitation of available sulfatases to break down the complex sulfation patterns of carrageenans poses a significant limitation for the sustainable production of valuable bioproducts from red algae. In this study, we screened several carrageenolytic polysaccharide utilization loci for novel sulfatase activities to assist the efficient conversion of a variety of sulfated galactans into the target product 3,6-anhydro-D-galactose. Inspired by the carrageenolytic pathways in marine heterotrophic bacteria, we systematically combined these novel sulfatases with other carrageenolytic enzymes, facilitating the development of the first enzymatic one-pot biotransformation of ι- and κ-carrageenan to 3,6-anhdyro-D-galactose. We further showed the applicability of this enzymatic bioconversion to a broad series of hybrid carrageenans, rendering this process a promising and sustainable approach for the production of value-added biomolecules from red-algal feedstocks.

| S-EPMC10958521 | biostudies-literature

Genome sequence of Vibrio sp. strain EJY3, an agarolytic marine bacterium metabolizing 3,6-anhydro-L-galactose as a sole carbon source.

Project description:The metabolic fate of 3,6-anhydro-L-galactose (L-AHG) is unknown in the global marine carbon cycle. Vibrio sp. strain EJY3 is an agarolytic marine bacterium that can utilize L-AHG as a sole carbon source. To elucidate the metabolic pathways of L-AHG, we have sequenced the complete genome of Vibrio sp. strain EJY3.

| S-EPMC3347216 | biostudies-literature

Effect of 3,6-anhydro-l-galactose on α-melanocyte stimulating hormone-induced melanogenesis in human melanocytes and a skin-equivalent model.

Project description:3,6-Anhydro-l-galactose (l-AHG) is a bioactive sugar that is a major component of agarose. Recently, l-AHG was reported to have anti-melanogenic potential in human epidermal melanocytes (HEMs) and B16F10 melanoma cells; however, its underlying molecular mechanisms remain unknown. At noncytotoxic concentrations, l-AHG has been shown to inhibit alpha-melanocyte-stimulating hormone-induced melanin synthesis in various cell models, including HEMs, melan-a cells, and B16F10 cells. Although l-AHG did not inhibit tyrosinase activity in vitro, reverse transcription-polymerase chain reaction results demonstrated that the anti-melanogenic effect of l-AHG was mediated by transcriptional repression of melanogenesis-related genes, including tyrosinase, tyrosinase-related protein-1 (TRP-1), tyrosinase-related protein-2 (TRP-2), and microphthalmia-associated transcription factor (MITF) in HEMs. Western blot analysis showed that l-AHG effectively attenuated α-melanocyte-stimulating hormone-induced melanogenic proteins by inhibiting cyclic adenosine monophosphate/cyclic adenosine monophosphate-dependent protein kinase, mitogen-activated protein kinase, and Akt signaling pathways in HEMs. Topical application of l-AHG significantly ameliorated melanin production in a 3D pigmented human skin model. Collectively, these results suggest that l-AHG could be utilized as novel cosmetic compounds with skin-whitening efficacy.

| S-EPMC6175185 | biostudies-literature

NADP<sup>+</sup>-Dependent Dehydrogenase SCO3486 and Cycloisomerase SCO3480: Key Enzymes for 3,6-Anhydro-L-Galactose Catabolism in <i>Streptomyces coelicolor</i> A3(2).

Project description:Agarose is a linear polysaccharide composed of D-galactose and 3,6-anhydro-L-galactose (AHG). It is a major component of the red algal cell wall and is gaining attention as an abundant marine biomass. However, the inability to ferment AHG is considered an obstacle in the large-scale use of agarose and could be addressed by understanding AHG catabolism in agarolytic microorganisms. Since AHG catabolism was uniquely confirmed in Vibrio sp. EJY3, a gram-negative marine bacterial species, we investigated AHG metabolism in Streptomyces coelicolor A3(2), an agarolytic gram-positive soil bacterium. Based on genomic data, the SCO3486 protein (492 amino acids) and the SCO3480 protein (361 amino acids) of S. coelicolor A3(2) showed identity with H2IFE7.1 (40% identity) encoding AHG dehydrogenase and H2IFX0.1 (42% identity) encoding 3,6-anhydro-L-galactonate cycloisomerase, respectively, which are involved in the initial catabolism of AHG in Vibrio sp. EJY3. Thin layer chromatography and mass spectrometry of the bioconversion products catalyzed by recombinant SCO3486 and SCO3480 proteins, revealed that SCO3486 is an AHG dehydrogenase that oxidizes AHG to 3,6-anhydro-L-galactonate, and SCO3480 is a 3,6-anhydro-L-galactonate cycloisomerase that converts 3,6-anhydro-L-galactonate to 2-keto-3-deoxygalactonate. SCO3486 showed maximum activity at pH 6.0 at 50°C, increased activity in the presence of iron ions, and activity against various aldehyde substrates, which is quite distinct from AHG-specific H2IFE7.1 in Vibrio sp. EJY3. Therefore, the catabolic pathway of AHG seems to be similar in most agar-degrading microorganisms, but the enzymes involved appear to be very diverse.

| S-EPMC9706016 | biostudies-literature

Reagent-Free Colorimetric Assay for Galactose Using Agarose Gel Entrapping Nanoceria and Galactose Oxidase.

Project description:A reagent-free colorimetric method for galactose quantification using a composite of cerium oxide nanoparticles (nanoceria) and galactose oxidase (Gal Ox) entrapped in an agarose gel was developed. In the presence of galactose, the Gal Ox entrapped within the agarose gel catalyzed the oxidation of galactose to generate H2O2, which induced a color change from white to intense yellow. This reaction occurred without any chromogenic substrate. This color transition is presumed to be due to the H2O2-mediated alteration of the oxidation state of cerium ions present on the surface of the nanoceria. The intensity of color change was quantified by acquiring an image with a conventional smartphone, converting the image to cyan-magenta-yellow-black (CMYK) mode, and subsequently analyzing the image using the ImageJ software. Using this strategy, galactose concentration was specifically determined with excellent sensitivity of as low as 0.05 mM. The analytical utility of the assay was successfully verified by correctly determining diverse levels of galactose in human serum, which is enough to diagnose galactosemia, a genetic disorder characterized by the malfunctioning of enzymes responsible for galactose metabolism. The assay employing a hydrogel composite with entrapped nanoceria and Gal Ox, is a simple, cost-effective, and rapid colorimetric assay for galactose quantification, without using any chromogenic reagent. This cost-effective method has great potential for the diagnosis of galactosemia and is highly promising in comparison to the laborious instrumentation-based methods currently in use.

| S-EPMC7279418 | biostudies-literature

3,6-Anhydro-L-galactonate cycloisomerase from Vibrio sp. strain EJY3: crystallization and X-ray crystallographic analysis.

Project description:3,6-Anhydro-L-galactonate cycloisomerase (ACI), which is found in the marine bacterium Vibrio sp. strain EJY3, converts 3,6-anhydro-L-galactonate into 2-keto-3-deoxygalactonate. ACI is a key enzyme in the metabolic pathway of 3,6-anhydro-L-galactose (AHG). Study of AHG metabolism is important for the efficient fermentation of agar and biofuel production, because AHG is a sugar that is non-fermentable by commercial microorganisms. The aci gene from Vibrio sp. strain EJY3 was cloned, and the recombinant protein was overexpressed and crystallized in order to determine the structure and understand the function of the protein. The crystals diffracted to 2.2 Å resolution and belonged to space group P41212 or P43212, with unit-cell parameters a = b = 87.9, c = 143.5 Å. The Matthews coefficient was 2.3 Å3 Da-1, with a solvent content of 47%.

| S-EPMC5619742 | biostudies-literature

Hydrogenotrophs-Based Biological Biogas Upgrading Technologies.

Project description:Biogas produced from anaerobic digestion consists of 55-65% methane and 35-45% carbon dioxide, with an additional 1-2% of other impurities. To utilize biogas as renewable energy, a process called biogas upgrading is required. Biogas upgrading is the separation of methane from carbon dioxide and other impurities, and is performed to increase CH4 content to more than 95%, allowing heat to be secured at the natural gas level. The profitability of existing biogas technologies strongly depends on operation and maintenance costs. Conventional biogas upgrading technologies have many issues, such as unstable high-purity methane generation and high energy consumption. However, hydrogenotrophs-based biological biogas upgrading offers an advantage of converting CO2 in biogas directly into CH4 without additional processes. Thus, biological upgrading through applying hydrogenotrophic methanogens for the biological conversion of CO2 and H2 to CH4 receives growing attention due to its simplicity and high technological potential. This review analyzes the recent advance of hydrogenotrophs-based biomethanation processes, addressing their potential impact on public acceptance of biogas plants for the promotion of biogas production.

| S-EPMC9085624 | biostudies-literature

Method establishment for upgrading chemical markers in pharmacopoeia to bioactive markers for biological standardization of traditional Chinese medicine.

Project description:Quality surveillance on authentication, safety and efficacy of proprietary Chinese medicines (pCm) are certainly the top priorities for the industries. Nowadays, the quality control system adopted is mainly chemical marker-oriented, concerning basically the correct use of raw material and safety issues, while the biological activities of the chemical marker(s) are seldom considered. Hence, there is an undefined relationship between the amount of chemical markers and the claimed pharmacological activities. In view of the need in identifying appropriate markers for biological standardization of pCm products, the present study aimed to establish a systematic methodology for verifying whether the chemical marker of a traditional Chinese medicine (TCM) listed in Chinese Pharmacopoeia could be upgraded to a bioactive marker with certain efficacy in treating a particular disease. Our proposed methodology included a series of work on extraction, quantification, literature search and in vivo pharmacological experiments, in which the water extractability, biological effects at theoretical dose and oral bioavailability of the candidate chemical markers were all taken into consideration. The feasibility and implication of this bioactive markers verification methodology were further elaborated. Our findings will serve as the foundation for further research and development of biological standardization of TCM.

| S-EPMC6544610 | biostudies-literature

1,5-Anhydro-3,6-di-O-benzyl-2-de-oxy-1,2-C-dichloro-methyl-ene-d-glycero-d-gulo-hexitol.

Project description:In the title compound, C(21)H(22)Cl(2)O(4), the pyranosyl ring adopts a twist-boat conformation with the O-benzyl groups in equatorial positions. In the crystal, O-H⋯O hydrogen bonding results in infinite chains of mol-ecules along [100]. The structure is further consolidated by weak C-H⋯O, C-H⋯Cl and C-H⋯π inter-actions. The absolute structure was determined.

| S-EPMC3247618 | biostudies-literature

7-Azido-N,N-diethyl-4,5-O-isopropyl-idene-4-C-methyl-3,6-anhydro-7-de-oxy-d-glycero-d-manno-heptonamide.

Project description:The reaction of 5-azido-5-de-oxy-2,3-O-isopropyl-idene-2-C-methyl-d-ribose with N,N-diethyl-2-(dimethyl-sulfuranyl-idene)acetamide gave the title compound, C(15)H(26)N(4)O(5), as the major product arising from initial formation of an epoxide which was subsequently opened by intra-molecular attack of the free 4-hydroxyl group. X-ray crystallography confirmed the relative stereochemistry of the title compound and the absolute configuration was determined by the use of d-ribose as the starting material. The crystal structure contains chains of mol-ecules running parallel to the a axis, being linked by weak bifurcated O-H?(N,N) hydrogen bonds.

| S-EPMC2968166 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data