Extraction, Purification, Structural Characteristics, Biological Activities, and Applications of Polysaccharides from Gastrodia elata: A Review
Abstract
:1. Introduction
2. Extracting and Purifying Techniques of G. elata Polysaccharides
2.1. Extraction and Separation of G. elata Polysaccharides
2.2. Purification of G. elata Polysaccharides
3. Structural Characteristics of G. elata Polysaccharide
4. Biological Activity of G. elata Polysaccharide
4.1. Anti-Cancer Activity
4.2. Immunomodulatory Activity
4.3. Antioxidant/Anti-Aging Activity
4.4. Antiviral/Antibacterial/Anti-Inflammatory Activity
4.4.1. Anti-Inflammatory Activity
4.4.2. Antibacterial Activity/Improvement of Intestinal Flora
4.4.3. Antiviral Activity
4.5. Neuroprotective Effects
4.6. Treatment of Cardiovascular Diseases
4.7. Other Activities
5. Structure–Activity Relation in G. elata Polysaccharide
6. Application of G. elata Polysaccharide
6.1. In the Food Industry
6.2. In the Pharmaceutical Industry
6.3. In the Cosmetics Industry
7. Conclusions and Future Prospects
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
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Extraction | Purification | ||||||||
---|---|---|---|---|---|---|---|---|---|
Polysaccharide Fraction | Extraction Method | Time | Temperature (°C) | Solid-Liquid Ratio (g/mL) | Power/Enzyme | Total Production (%) | Polysaccharide Fraction | Purification Method | Ref. |
GEPs | Hot water extraction | 2 h | 1:10 | 58.4 | Deproteinization using Sevag method; the crude polysaccharides were decolorized by using the D101macroporous resin | [48] | |||
GaE-B GaE-R GaE-Hyb GaE-G | Water extraction | 4 h | 90 | 1:20 | GaE-B: 5.67 GaE-R: 4.21 GaE-Hyb: 6.63 GaE-G: 7.82 | Sevag reagent to remove the associated protein; Dialysed in a dialysis bag with flowing distilled water | [30] | ||
GBP | Water extraction and ethanol precipitation methods | 1 h | 60 | 1:30 | Deproteinization by Sevag method; dialysis was performed using a 3500 Da dialysis membrane. | [31] | |||
Ultrasonic Assisted Extraction | 1 h | 70 | 1:30 | 160 w | Wash three times with ethanol and acetone, centrifuge for 10 min and collect the sediment. | [49] | |||
GEP-3; GEP-4 | Hot water extraction | 4 h | 70 | 1:30 | GEP-3; GEP-4 | Precipitation and deproteinisation using the Sevage method; DEAE-cellulose column; Sephacryl 200 column; 5 kDa membrane separation equipment. | [14] | ||
PGE-20, PGE-40, and PGE-120 | Ultrasonic assisted extraction with deionized water | 20, 40, and 120 min | 70 | 1:30 | 200 w | PGE-20, PGE-40, and PGE-120 | Add 95% ethanol and leave overnight at 4 °C for polysaccharide precipitation. | [19] | |
GEP-1 | Water extraction and alcohol precipitation | 11.11 | GEP-1 | Separate using a 10 kDa membrane separation device and elute with water. | [24] | ||||
GEP-D GEP-1 | Hot water extraction | GEP-D: 0.89 GEP-1: 0.67 | GEP-D GEP-1 | Sevag solvent for protein removal; DEAE-Sepharose Fast Flow column; Sephacryl S-400HR column. | [43] | ||||
GEP | water extraction | 4 h | 100 | 1:15 | GEP | Removing proteins using Sevag method. | [50] | ||
GEP | water extraction | 4 h | GEP | Ethanol precipitation, deproteinised by Sevag method, dialysed in 3000 Da dialysis bag. | [45] | ||||
SGEP AcGEP | Ultrasonic assisted extraction with deionized water | 30 min | 70 | 1:30 | 200 w | 95% ethanol precipitation. | [19] | ||
Hot water extraction | 1 h | 1:10 | Precipitation and washing with anhydrous ethanol and acetone followed by chloroform/butanol to remove proteins. | [45] | |||||
GEP, GEP-SA, GEP-Cy5.5 | Boiling water extraction | 2 h | 1:30 | GEP, GEP-SA, GEP-Cy5.5 | Precipitate with anhydrous ethanol and remove protein 6–7 times with Sevag reagent; DEAE-52 cellulose. | [50] | |||
Ultrasonic extraction with distilled wate | 36 min | 56 | 1:59 | Anhydrous ethanol precipitation and Sevag method for deproteinization. | [35] | ||||
Se-GEP | Boiling water reflux extraction | Se-GEP | Protein removal by Sevag method; ethanol precipitation and centrifugation; use of DEAE-52 ion exchange resin columns. | [51] | |||||
PGE | Water extraction | 2 | 60 | 1:40 | 15.81 | PGE | Sepag method for deproteinization, Wash crude polysaccharides on Sephadex G-200 column, further purify with ultrafiltration tube. | [52] | |
PGB | Water extraction | DEAE-52 cellulose col umn (2.6 × 50 cm) chromatography separation and purification for the preparation of PGB. | [53] | ||||||
WGEW AGEW | Extract with boiling water | 4 h | WGEW: 11.76 AGEW: 18 | WGEW AGEW | DEAE cellulose column elution. | [23] | |||
GPs | Water extractionr | 4 h | GPs | Proteins were removed with 15% trichloroacetic acid, and then a column with DEAE-52 cellulose eluted the crude polysaccharides. | [54] | ||||
GEP | Thermostatic water bath extraction | 4 h | 90 | 1:10 | GEP | Protein removal by Sevag method; Precipitate in ethanol and filter through Whatman GF/A filter paper. | [55] | ||
WTMA | Boiling-water extraction | 4 h | WTMA: 0.69% | WTMA | Proteins were removed with trichloroacetic acid; the supernatant was dialysed; ethanol precipitation yielded crude polysaccharides, which were then eluted on a DEAE cellulose column. | [22] | |||
RGP-1a RGP-1b | 66 min | 74 | 1:54 | 6.11 | RGP-1a RGP-1b | SProtein removal by eaveg method, purification by DEAE cellulose-52 and Sephadex G-100 elution. | [56] | ||
Crude polysaccharides fraction Acidic polysaccharide fraction | Boiling water extraction | 3 h | 60 | 1:10 | Crude polysaccharides fraction: 2.47 Acidic polysaccharide fraction: 0.61 | Crude polysaccharides fraction Acidic polysaccharide fraction | The crude polysaccharide extract was further purified using ion exchange chromatography on DEAE Sepharose CL-6B. | [57] | |
Extraction with petroleum ether reflux | 2 h | 1:30 | Proteins were removed by the Seaveg method, decolourised by 1% activated carbon and the filtrate was left overnight; filtered and dried. | [58] | |||||
Add 80% ethanol for water bath reflux | 2 h | 60 | 1∶8 | Dehydrated ethanol precipitation of polysaccharides. | [59] | ||||
Hot water extraction | 30 min | 95 | 1:20 | Proteins were removed with lead acetate, ethanol precipitated and then processed by elution on a DEAE-52 cellulose column. | [60] | ||||
Boiling water extraction | 4 h | 1:75 | Anhydrous ethanol for alcohol precipitation | [61] | |||||
Hot water extractio | 45 min | 65 | 1:40 | 3.28 | Sevag method for deproteinization and alcohol precipitation drying. | [62] | |||
Ultrasonic assisted extraction of citrate buffer solution | 30 min | 50 | 1:40 | 300 w | Sevage method for deproteinization; Perform alcohol precipitation with 5 times the volume of methanol. | [63] | |||
Ultrasonic assisted water extraction | 34 min | 66 | 1:45 | Decolorize with hydrogen peroxide, precipitate with 95% ethanol, and wash with ether, petroleum ether, and anhydrous ethanol respectively. | [64] | ||||
Hot water extraction | 2.5 h | 70 | 1:37 | 22.38 | Anhydrous ethanol for alcohol precipitation. | [65] | |||
Petroleum ether degreasing followed by pure water extraction | 4 h | 100 | 1:15 | 1.21 | A mixture of chloroform and n-butanol was used for protein extraction and removal, and ethanol precipitation. | [33] | |||
GEP, GEP II, GEPs, and GEP IIs | Water extraction and alcohol precipitation method | DEAE-52 elution separation, Sephadex G-100 elution separation. | [66] | ||||||
SGCP2 SGCP3 NSGCP2 NSGCP3 | Hot water extraction | 31 min | 67 | 1:16 | SGCP2: 21.50 SGCP3: 26.65 NSGCP2: 10.94 NSGCP3: 10.28 | SGCP2 SGCP3 NSGCP2 NSGCP3 | Alcohol precipitation and protein removal by Sevag reagent, purification by dialysis, chromatography on DEAE-52 cellulose columns and Sephadex G-50 gel columns | [67] | |
PGEB-3-H | Pure water extraction | 3 h | 50 | PGEB-3-H | Ethanol precipitation, deproteinisation, dialysis; further purification by DEAE-52 cellulose column chromatography and Sephadex G-100 column chromatography. | [68] | |||
WPGB-A-H WPGB-A-L | Pure water extraction | 3 h | 50 | 1:10 | WPGB-A-H: 0.824% WPGB-A-L | WPGB-A-H WPGB-A-L | Sevag method for deproteinization, dialysis, ethanol precipitation, DEAE-52 cellulose chromatography, and Sephadex G-100 chromatography for separation and purification. | [69] | |
Water extraction and alcohol precipitation method | 3 h | 120 | 1:40 | The protein was removed by Sevag method and separated by Sepharose 6 Fast Flow gel. | [70] | ||||
Water extraction and alcohol precipitation method | 3 h | 120 | 1:40 | Proteins are removed by the Seaveg method, decolourised by activated carbon, filtered and the filtrate left overnight. | [71] | ||||
GEP1 GEP2 | Boiling water extraction | 2 h | 96 | GEP1: 20.8 GEP2: 25.4 | GEP1-G GEP2-G | Ethanol precipitation, Sevage method to remove protein, dialysis, purification. | [72] | ||
GEP GEP1 GEP2 | Pure water extraction | 2.5 h | 70 | 13.15 | GEP GEP1 GEP2 | 95% ethanol precipitation, Sevag method for deproteinization, activated carbon decolorization, DEAE-52 cellulose chromography elution | [73] | ||
Pure water extraction | 2 h | 80 | 1:30 | 13.46 | Anhydrous ethanol for alcohol precipitation | [74] | |||
Degreased with petroleum ether and extracted by reflux in a water bath | 4 h | 100 | 1:40 | Deproteinised and precipitated. The precipitate was washed with anhydrous ethanol and acetone. | [75] | ||||
Water bath reflux extraction | 2 h | 90 | 1:8 | Anhydrous ethanol for alcohol precipitation. | [76] | ||||
Water extraction and alcohol precipitation | 1 h | 1:30 | Sevag method for deproteinization and retention of relative molecular weight 1000 in dialysis bags, dialyzed in water for 24 h. | [77] | |||||
Water extraction and alcohol precipitation method | 2 h | 80 | 1:40 | 9.61 | Dialysis using dialysis bags, alcohol precipitation and Sepharose 6-Fast Flow gel column chromatography elution. | [27] | |||
Pure water extraction | 3 h | 120 | 1:40 | Protease degradation + sevag method for protein removal. | [78] | ||||
TM-20, TM-40, TM-60 | Hot water extraction | 3.1 h | 90 | 1:32 | TM-20, TM-40, TM-60 | Ethanol fractional precipitation. | [79] | ||
Water bath reflux extraction | 2 h | 80 | Ethanol precipitation, protein removal by enzymatic hydrolysis Sevag method, decolourisation with H2O2, dialysis with distilled water. | [46] | |||||
YGEP SGEP | Ultrasonic assisted hot water extraction | 1 h | 70 | 1:30 | The polysaccharides were precipitated, washed, and then eluted by flow fractionation with an asymmetric flow field. | [80] | |||
Water extraction and alcohol precipitation | 2 h | 50 | Sevag method for protein removal and activated carbon for pigment removal, DEAE cellulose column for elution. | [81] | |||||
GEP SeGEP | Hot water extraction | 2 h | 80 | 1:30 | GEP SeGEP | Sevag reagent (chloroform: n-butanol = 4:1) was used to remove free proteins, followed by precipitation with anhydrous ethanol. | [82] | ||
Ultrasonic assisted water extraction | 48 min | 78 | 1:16 | 17. 22 | Extracted with trichloromethane n-butanol and precipitated with ethanol. The residue was washed with ethanol, acetone and ether. | [83] | |||
GBP-Ⅰ, GBP-Ⅱ | Hot water extraction | 6 h | GBP-I, GBP-II | filtered, deproteinised by the Sevag method and washed repeatedly with anhydrous ethanol, acetone and ether. | [84] | ||||
Water bath extraction method | 4 h | 100 | 1:30 | Protein removal with chloroform n-butanol and alcohol precipitation with anhydrous ethanol. | [85] | ||||
Water extraction and alcohol precipitation | 2 | 60 | 1:40 | 15.81 | Enzyme + Sevag method combined to remove proteins, and Sephadex G-200 combined with ultrafiltration tube for separation and purification. | [86] | |||
GeB40-1 GeB80-4 | Water extraction | 36 min and 34 min | 58 and 66 | 1:37 and 1:45 | 9.25, 32.78 | GeB40-1 GeB80-4 | Ethanol fractionation, papain + Sveg method for protein removal, dialysis method, DEAE-52 cellulose column chromatography. | [87] | |
WTM-1,WTM-2, WTM-3, WTM-4, WTM-5, WTM-6 | Water extraction and alcohol precipitation | 2 h | 60 | 1:30 | 5.47 | WTM-1,WTM-2, WTM-3, WTM-4, WTM-5, WTM-6 | Protein removal by the Sevage method, removal of small molecule magazines and pigments by hollow fibre ultrafiltration membranes, separation and purification by DEAE-52 and Sephadex G-100. | [88] | |
WPGB-A-H | Water bath extraction | 3 h | 50 | 1:10 | 0.824 | Sevag method for deproteinization, dialysis, ethanol precipitation, DEAE cellulose and Sephadex G-100 chromatographic separation and purification. | [89] | ||
PRG1 PRG2 PRG3 PRG4 PRG5 | Water extraction and alcohol precipitation | 65 min | 78 | 1:51 | Colour was removed using activated charcoal, proteins were removed using the sevage method, dialysed using distilled water, precipitated with alcohol and further purified using cellulose DE-52 and gel G-100. | [90] | |||
Water extraction and alcohol precipitation, Ultrasound assisted alcohol extraction | 3 h and 1 h | 60, 50 | 1: 60 | Degreased and decolorized with petroleum ether and anhydrous ethanol, precipitated with ethanol, removed protein by Sevage method, and dialyzed with deionized water. | [91] | ||||
TM1 TM2 TM3 | Water extraction and alcohol precipitation | 2 h | 50 | TM1 TM2 TM3 | Sevag method for deproteinization, dialysis with distilled water, precipitated by ethanol, washed several times with organic reagents, and chromatographed on a DEAE (OH−) cellulose column (2.6 × 50 cm). | [92] | |||
GB I-1 GB I-2 GB I-3 GB II GB III GB IV GB V | Boiling water extraction | 6 h | GB I-1 GB I-2 GB I-3 GB II GB III GB IV GB V | GB I-1 GB I-2 GB I-3 GB II GBIII GBIV GB V | DEAE Sepharose Fast Flow ion exchange chromatography, SephadexG-10 column desalination, molecular sieve gel column chromatography elution, and then SephadexG-10 desalination. | [93] |
Polysaccharide Fraction | Configuration | Molecular Weights/Molecular Mass | Monosaccharide Composition | Structural Characteristic | Analytical Techniques | Bioactivities | Ref. |
---|---|---|---|---|---|---|---|
GEPs | 292.596 kDa | Glu:Gal:GalA:Ara:Fru = 88.21: 4.48: 4.40:0.87:0.85 | HPGPC, MALLS, 1260 HPLC, HPAE-PAD | Strong immune-enhancing effects | [48] | ||
GBP | 53.43 ± 0.83 | Glu:Fru = 8.7:1 | GPC-MALLS-RI,HPLC, HPLC-RI. | Neuroprotective effects. | [99] | ||
GEP-3 GEP-4 | GEP-3: 20 kDa GEP-4: 25 kDa | Glu | GEP-3: 1,4-glucan GEP-4: →[4)-α-Glcp-(1]10→[4)-α-Glcp-(1→]5[6)-β-Glcp-(1]11→6)-α-Glcp-(3→ and two branches of β-Glcp and p-hydroxybenzyl alcohol citrate, with repeating p-hydroxybenzyl alcohol attached to the backbone chain at O-6 position of →4,6)-α-Glcp-(1→ and O-1 position of →3,6)-α-Glcp-(1→. | HPGPC, PMP-HPLC, LC/MS, FT-IR, NMR, SEM. | Promote the growth of Akkermansia muciniphila. | [14] | |
RGP-1a RGP-1b | RGP-1a: 19.25 kDa RGP-1b: 3.92 kDa | RGP-1a: Fru:Glu = 1:10.68 RGP-1b: Glu | HPLC-RID, HPGPC, FTIR. | Immunological activity. | [56] | ||
GEP-1 | 20.15 kDa | Glu | The fully O-methylated GEP-1 was composed of 2,3,4,6-Me4-Glcp, 2,3,6-Me3-Glcp, 2,3,4-Me3-Glcp, 2,3-Me2-Glcp and 2,6-Me2-Glcp with a molar ratio of 2.23:9.69:4.93:1.08:2.07. | HPGPC, PMP-HPLC, LC/MS, FT-IR, NMR, SEM. | Promote the growth of Akkermansia muciniphila. | [24] | |
GEP-1 | α | 76.444 kDa | Glu:Gal:Ara:Man = 92.04:4.79:2.19:0.34 | α-(1→4)-glucans. | Enhancing immune. | [43] | |
GEP | 42.58 × 104 Da | Glucose, Galactose and Galacturonic acid | α-glucopyranose structure. | HPGPC, HPIC, FT-IR. | Neuroprotective effects. | [100] | |
GEP SGEP AcGEP | GEP: 12.9 × 107 g/mol SGEP: 9.3 × 107 g/mol AcGEP: 9.3 × 107 g/mol | FT-IR, AF4-MALS-dRI. | Anti-Breast Cancer Activity. | [19] | |||
GEP2–6 | 2.7 × 106 Da | Glu | GEP2–6 was a glucan linked by α-(1 → 4) and α-(1→6) glycosidic bonds. | HPGPC/SEC, UPW, HPLC-ELSD, FT-IR, GC-FID, NMR, AFM. | Antioxidant. | [45] | |
GEP | 12 kDa | Glu:Gal = 82.33:1.0 | High-performance ion exchange chromatography, FT-IR, UV, NMR. | [50] | |||
G. elata Bl. F. elata G. elata Bl. F. Glauca S Chow G. elata Bl. F. Viridls MalKino | G. elata Bl. F. elata: Glu:Gal:GalUA:Man:Ara:Rha = 29.16:28.89:13.85:9.81:8.17:6.20 G. elata Bl. F. Glauca S Chow:Glu:Gal:GalUA:Man:Ara:Rha = 37.32:26.29:10.97:4.69:4.10:4.37 G. elata Bl. F. Viridls MalKino: Glu:Gal:GalUA:Man:Ara:Rha = 21.84:30.78:14.76:9.30:9.65:4.18 | HPAEC. | Antioxidant activity. | [35] | |||
GEP Se-GEP | GEP: 524.4 kDa Se-GEP: 488.9 kDa | Glu | UV, FT-IR, HPLC, SEM, EDX, HPGPC. | [51] | |||
PGE | 1.54 × 103 kDa | Glu | PGE was composed of (1→4)-linked-glucose. Residues of branch structure might be (1→4,6)-linked-glucose, (1→3)-linked-glucose and T-glucose. | HPLC, UV, FT–IR, NMR, GC–MS. | Inhibiting ACE activity. | [52] | |
WGEW AGEW | α | WGEW: 1.0× 105 AGEW: 2.8 × 105 | Glu | α-d-(1→4)-glucan with an α-(1→4) linked branch attached to O-6 branch points with different branch degrees. | GC, GC-MS, NMR. | Anti-dengue virus bioactivities. | [23]. |
GPs | 2.71 × 105 Da | Glu | HPSEC. | Immune modulating activities. | [54] | ||
GEP | 875.19 kDa | Glu | FT-IR, UV, LC-10A. | Antioxidant activity. | [55] | ||
WTMA | 7.0 × 105 Da | Glu | α-1→4)-glucan with α-(1→4) linked branches attached to 0–6 at branch points. | HPGPC, GC, GC–MS, NMR, MALDI-TOF. | Antitumor. | [22] | |
PGEB-3H | 28.8 kDa | Glu | PGEB-3H was mainly composed by glucose, and had a (1→4)-α -d-glucan main chain occasionally branched with α-1,6 glycosidic linkage. | PC, GC, HPGPC, IR, NMR. | Hypolipidemic Activity. | [97] | |
SGCP2 SGCP3 NSGCP2 NSGCP3 | SGCP2: 31,027 Da SGCP3:727,650 Da NSGCP2: 39,812 Da NSGCP3: 39,991 Da | SGCP2: Man:Rha:GlcA:Glc:Ara = 1.99:1.72:3.60:70.68:22.01 SGCP3: Man: Rha:GlcA:Glc:Ara = 1.19:1.06:2.30:73.81:21.64 NSGCP2: Man:Rha:GlcA:Glc:Xyl:Ara = 2.96:1.39:3.08:70.05:0.63:21.88 NSGCP3: Man:Rha:GlcA:Glc:Ara = 0.86:0.99:2.03:74.47:21.65 | SGCP2, SGCP3 and NSGCP2, NSGCP3 are both composed of three glycosidic bonds, namely: d-Glcp-1 →, → 4) - d-Glcp - (1 → and → 4,6) - d-Glcp - (1 →). The main chain connection of polysaccharides SGCP3 and NSGCP3 is → 4) - α - d-Glcp - (1 →, while the terminal group α - d-Glcp - (1 → is connected to the main chain through an O-6 bond. | UV, HPGPC, FT-IR, GC-MS, HPLC. | Antioxidant activity. | [67] | |
GPSa | 4.23 × 105 Da | Rha: Man: Glu = 1:1.07:67.24 | The main structure of the sugar chain is α— (1→4) pyranose type d-glucose. | HPLC, IR, NMR. | [26] | ||
YGEP AcYGEP | GEP is a pyranose, mainly d-glucose linked by alpha glycosidic bonds. | AF4-MALS-dRI,UV/Vis, FTIR, XRD, SEM. | [80] | ||||
GBI-1 GBI-2 GBI-3 GBII GBIII GBIV GBV | GBI-1: 14,600 GBI-2: 8700 GBI-3: 7000 GBII: 4300 GBIII: 19,000 GBIV: 87,000 GBV: 100,000 | HPLC, GC-MS, FT-IR. | Treatment of acute liver injury. | [93] | |||
GEP SeGEP | α | β–glycosidic bond linked polysaccharide structure with pyran ring as skeleton. | UV, FT-IR, HPLC, NMR, SEM. | Antioxidant activity. | [82] | ||
PGE | α | 1.54 × 103 kDa | Glu | Alpha type d-glucose, with a pyran ring configuration, is mainly linked by glycosidic bonds with glucose as the main chain, and branches may include glucose with 1→3 linkage, glucose with 1→4→6 linkage, and glucose with 1 → linkage at the end. | HPLC, FT-IR, UV, NMR, ESM. | [86] | |
GeB40-1 GeB80-4 | α | Greater than 8000 Da | GeB40-1:L-rhamnose:D-galactose:D-glucose:D-xylose:D-mannose = 29:1:42:11:2 GeB80-4:L-rhamnose:D-galactose:D-glucose = 2.5:1:25 | α-glycosidic bond. | UV, HPLC, HPAEC. | Antibiotic activity. | [87] |
WTM-2 WTM-3 WTM-5 WTM-6 | α | WTM-2: 40.41 KDa WTM-3: 30.43 KDa WTM-5: 17.02 KDa WTM-6: 12.76 KDa | WTM-2:glucose:xylose:fructose:glucuronic acid = 72.43:4.12:1.00:0.24 WTM-3:glucose:xylose:fructose:glucuronic acid = 74.21:3.19:1.00:0.25 WTM-5:glucose:xylose:fructose:glucuronic acid = 70.07:5.13:1.00:0.34 WTM-6:glucose:xylose:fructose:glucuronic acid:mannose:= 69.62:0.57:1.00:0.35:0.24 | (α-d-Glcp-(1→4)-α-d-Glcp)n. | HILIC-ELSD, UV, IR, NMR, SEM, XRD. | Antineoplastic activity. | [88] |
WPGB-A-H | α | 28,840 Da | Two kinds of monosaccharide composition of D-glucose and D-mannose. | α-type dextran, sugar ring configuration is pyran type. | HPLC, IR, UV, GC. | [89] | |
PRG1 PRG2 PRG3 | α | PRG1: 19,251 Da PRG2: 3920 Da PRG3: 32,646 Da | PRG1: Fru: Glu = 1:10.682 PRG2: Glu PRG3: Fru: Glu = 1:1.542 PRG4: PRG5: Formed by dehydration condensation of glucose | The glycosidic bonds are all α-configuration. | HPGPC, HPLC, IR, UV. | Antioxidant activity. | [90] |
TM1 | 2.02 × 105 Da | Rha:Fuc:Xyl:Man:Glu = 0.22:14.80:0.36:39.00:66.52 | It is composed of α (1-6)-d-Glc, containing a small amount of β-configuration, and the side chain branch point is at the C-4 position. | UV, GC, IR, NMR. | [92] |
Biological Activities | Polysaccharide Name | CELL LINE | Modelling | In Vivo/In Vitro | Dosages | Mechanism of Action | Ref. |
---|---|---|---|---|---|---|---|
Anti-cancer activity | |||||||
pancreatic cancer | WTMA | PANC-1 and LO2 | —— | In vitro | —— | Anti-cancer activity assay indicated that the polysaccharide could inhibit the growth of PANC- 1 cell. | [22] |
Breast Cancer | GEP | MCF-7 cell | —— | In vitro | —— | The MCF-7 cell cycle was arrested at the S phase after AcGE treatment | [19] |
antitumor | PGEs | MCF-7cell | —— | In vitro | 0, 1, 2, 4, 6 mg/mL | The PGEs can inhibit the growth of MCF-7 cells by inducing late apoptosis. | [107] |
glioma resistance | PGEs | Rat glioma cells (C6) | —— | In vivo | 0.10, 0.25, 0.50, 1.00, 1.50 mg/mL | Inhibition of active migration in glioma cell growth. | [108] |
pheochromocytoma (blood cell tumour) | PGEs | PC12 cell line | —— | In vivo | 0, 250, 500, 1000 μg/mL | Inhibits intracellular Ca2+ concentration overload, regulates the BCL-2/BAX ratio, and inhibits caspase pathways. | [79] |
Transplantable tumours | PGEs | S180 sarcoma and H22 hepatocellular carcinoma strains | —— | In vivo | 0.8, 0.4, 0.2 g/kg | Destruction of tumour cell proliferation and enhancement of body immunity in hormonal mice, etc. | [109] |
liver cancer | PGEs | Mouse Hepatocellular carcinoma H22 cell | —— | In vivo | 30, 60, 90 mg/kg | Affects the BCL-2/BAX-Caspase pathway in PC12 cells and regulates the mitochondrial apoptotic pathway. | [110] |
loaded tumor | PGEs | H22 cell | —— | In vivo | 320, 160, 80 mg/kg | It affects cell cycle distribution, inhibits cell proliferation and activates the caspase system to induce apoptosis in tumour cells. | [111] |
liver cancer | WSS25 | RAW264.7 or BMM | RANKL treatment to induce osteoclastogenesis in mice | In vivo/in vitro | —— | WSS25 inhibits RANKL-induced osteoclast formation in RAW264.7 cells and BMM by blocking the BMP-2/Smad/Id1 signalling pathway | [112] |
colorectal cancer | PGEs | SW480 (Human colon cancer cell lines) | —— | In vitro | 500, 1000 μmol/mL | G. elata polysaccharide promotes the expression of miR-27a-3p and inhibits the expression of B7-H3 | [46] |
Immunomodulation | |||||||
Immunostimulatory Effect | PGEs | RAW264.7 Cells | Lipopolysaccharide inflammation model | In vitro | 50, 100, 200 μg/mL | By activation of the NF-κB signaling pathway | [43] |
Immnue-enhancing activity | PGEs | —— | Intragastric administration of cyclophosphamide | In vivo | 10 mL/kg | Improved the serum IL-2, TNF-a, IFN-g, IgG, IgA and IgM levels as well as the spleen and thymus indexes | [53] |
immunomodulatory activity | PGEs | —— | a mouse model of CTX-induced immunosuppression | In vivo | 200, 400 mg/kg | The modulation of the com position of gut microbiota by GEPs and the resulting increased content of SCFAs. | [48] |
Immunomodulatory Effects | SeGEP | RAW264.7 Cells | Cyclophosphamide-Treated Mice | In vivo/in vitro | 5, 10, 15, 20 μg/mL | Se-GEP treatment enhanced cell viability and phagocytosis and increased the secretion levels of NO and TNF-α. | [50] |
Neuroprotectiv effect | GEP | PC12 cell | A dose of 200 µmol/l CORT was selected to induce PC12 cell apoptosis | In vitro | 250, 500, 1000 µg/mL | By inhibiting oxidative stress and ER stress-mediated apoptotic pathways. | [113] |
low immune function | PGEs | —— | CTX-induced immuno suppressive mouse model | In vivo | 100, 200, 400 mg/kg | Significantly increases serum IgA, IgG, IgM and serum solubility. haemoglobin levels, increased spleen index and thymus index. | [114] |
immune liver injury | PGE-2 | —— | Immune liver injury model induced by BCG + LPS in mice | In vivo | 25, 50, 100 mg/kg | The hepatoprotective mechanism of GEP-2, may be through the production of homeostatic cytokines and the modulation of body immune function | [115] |
Immunological Activity | RGP-1a and RGP-1b | RAW 264.7 | cytotoxicity assay | In vitro | 200 µg/mL | RGP-1a and RGP-1b significantly affected RAW 264.7 NO generation and phagocytic activity in a dose-dependent manner. | [55] |
anti-ageing | |||||||
antioxidant activity analysis | PGEs | —— | —— | In vitro | 1, 2.5, 4, 5.5, 6 mg/mL | The polysaccharide concentration was 1.0 mg/mL, the scavenging rates of DPPH and ABTS free radicals were both over 80%. | [35] |
antioxidant | SeGEP | —— | —— | In vitro | 10 mg/mL | DPPH free radical scavenging rate and ABTS free radical cation scavenging rate. | [82] |
anti-ageing | PGEs | —— | Aging model of mice injected with 5% D-galactose | In vivo | 2.5, 5.0, 10.0 mg/(g.d) | SPGEs can improve the learning and memory ability of mice, DPPH free radical scavenging rate and ABTS free radical cation scavenging rate. | [116] |
antioxidant | GEP-G GEP2 G | —— | —— | In vitro | 1 mg/mL | Increased DPPH clearance, superoxide anion inhibition and hydroxyl radical inhibition. | [74] |
antioxidant | PGEs | —— | —— | In vitro | 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5 mg/mL | Improve the scavenging efficiency of DPPH free radical and hydroxyl radical. | [62] |
anti-ageing | PGEs | —— | The aging mouse model was established by subcutaneous injection of 5% D-galactose (125 mg/kg). | In vivo | 0.4, 2.0, 10.0 mg/(g·d−1) | Its mechanism may be related to the down-regulation of caspase-3, MAFbX and MURF-1 expression. | [117] |
Antiviral/antibacterial/anti-inflammatory | |||||||
cerebral ischemia–reperfusion injury | NPGE | HT22 cell | mouse model of ischemic stroke (IS) | In vivo/in vitro | 100, 250, 500 μg/mL | It inhibited neuroinflammation by down-regulating the level of IL-1β, IL-6, TNF-α, NLRP3, and HMGB1. | [118] |
Akkermansia muciniphila | GEP-3, GEP-4 | Mucococcus spp. | HFD and NASH mice | In vivo/in vitro | —— | GEP-1 could promote the growth of A. muciniphila and L. paracasei strains. | [14,24] |
Inflammatory bowel disease | GBP | —— | dextran sulfate sodium (DSS)-induced IBD mice | In vitro | 70 mg/kg | GBP treatment restores imbalances in the gut microbiota by increasing levels of beneficial bacteria. | [31] |
Gut Microbiota | GEP-I | intestinal flora | simulated intestinal fluid (SIF), | In vitro | 10 mg/mL | GEP-I promotes the growth of probiotics, inhibits the number of pathogenic bacteria, and significantly increases the concentration of acetic acid, etc., thus acting as a prebiotic. | [44] |
anti-inflflammatory and neuroprotective effffects | GBP | —— | Animal Model of Neuropathic Pain | In vivo | 20 mg/kg | Suppression of neuroinflammation. | [99] |
anti-dengue virus bioactivities | WGEW, AGEW | anti-dengue virus (Aedes albopictus C6/36 cells) | —— | In vitro | —— | WSS45 and WAS45 exhibited a protective effffect on dengue virus as indicated by the absence of CPE in in-fected C6/36 cells. | [23,56] |
Dengue 2 virus | WSS45 | BHK cells | dengue virus serotype 2 (DV2), | In vitro | —— | WSS45 exerted potent inhibitory effect on DV2 through interfering with the interaction between viruses and targeted cells. | [119] |
short-chain fatty acid | PGEB-3-H | intestinal flora | SD rats were experimental model. | In vivo | 100, 200, 400 mg/(kg·d) | Medium and low dose additions of G. elata polysaccharides had a more pronounced effect on SCFA concentration. | [120] |
Neuroprotection | |||||||
Neuroprotectiv effect | PGEs | PC12 cell | PC12 cell apoptosis induced by corticosterone (CORT) | In vitro | 250, 500, 1000 mg/mL | Neuroprotective effects of GEP depend on inhibition of endoplasmic reticulum stress-mediated pathways. | [113] |
neural protective | PGEs | —— | The model was prepared by middle cerebral artery occlusion (MCAO) | In vivo | 100 mg/kg | Reduction of cytokine TNF-α and IL-1β mRNA expression in the hippocampus and improvement of hippocampal neuronal function | [53] |
antidepressant | PGEs | —— | Lipopolysaccharide (LPS) -induced depressive mice | In vivo | —— | GEPS improves survival from CORT-induced PC12 cell injury and reduces LDH release from damaged cells | [121] |
nerve damage | PGEs | PC12 cell | Corticosterone-induced PC12 cell injury | In vitro | 250, 500, 1000 μg/mL) | GEPS increased the survival rate of CORT-induced damaged PC12 cells and decreased the release rate of LDH. | [77] |
cerebral palsy | PGEs | —— | The cerebral palsy model was established by ligation of the left common carotid artery and hypoxia for 1 h in young rats. | In vivo | 300, 150 mg/kg | The mechanism is related to the increase of NO, NE and 5-HT in the cerebral cortex and hippocampus, the decrease of ACHE level, the increase of eNOS expression and the protection of hippocampal tissues. | [122] |
Glutamate damaged HT22 cells | PGEs | HT22 cell | HT22 cells were incubated with 50 μg·mL−1 glutamate for 6 h. | In vitro | 12.5, 25, 50, 100, 200 μg/mL | The mechanism may be related to the up-regulation of HO-1 expression and improvement of cellular antioxidant capacity. | [123] |
Cerebral ischemia | PGEs | —— | The rat model of permanent focal cerebral ischemia was established by embolizing the right middle cerebral artery. | In vivo | 100 mg/kg | The mechanisms may play a protective role for neurons in the ischemic region by promoting the proliferation of endogenous NSCs. | [124,125] |
Brain nerve cells | PGEs | —— | Young rat model of cerebral palsy. | In vivo | 300 mg/kg | Significantly inhibited apoptosis in cerebral tissue of young rats with cerebral palsy | [126] |
Cardiovascular system activity | |||||||
Spontaneously Hypertensive | Acidic Polysaccharides | —— | Spontaneously hypertensive rats (SHR) fed with high fat diet. | In vivo | 6 mg/kg | acidic polysaccharides from Gastrodia rhizome reduce hypertension and improve serum lipid levels. | [57] |
Suppression of serum cholesterol | PGEs | —— | rats fed a high-fat diet | In vivo | 6 mg/kg | Significantly suppresses the risk of atherosclerosis by reducing serum total cholesterol and LDL levels in SD rats. | [127] |
Non-alcoholic fatty liver disease | PGEs | —— | High-fat diet induced model | In vivo | 50, 100, 200 mg/kg | Inhibition of NF-κB, TNF-α, IL-1β, iNOS and COX-2 protein expression in liver tissue, and inhibition of Bax expression, up-regulation of Bcl-2 factor. | [76] |
lowering of blood pressure | PGEs | —— | Hypertensive rat model (RHR). | In vivo | 50, 100, 200 mg/kg ·d | The mechanism of action is related to promoting the production of endogenous vasodilators and inhibiting the release of endogenous vasoconstrictors. | [128] |
Other roles | |||||||
osteoclast differentiation | WSS25 | RAW264.7 cells or mouse bone marrow macrophages (BMMs) | RAW264.7 cells or mouse bone marrow macrophages (BMMs) to induce osteoclastogenesis. | In vitro | 2.5, 5, 10 µg/mL | WSS25 inhibits RANKL-induced osteoclast formation in RAW264.7 cells and BMMs by blocking the BMP-2/Smad/Id1 pathway. | [112] |
anti-vertigo | PGEs | —— | Dizziness in mice caused by mechanical rotation | In vitro | —— | GEP and AMP were similar in activity, and both significantly reduced the time taken by stunned mice to escape from electric shock (p < 0.01) and increased the amount of food consumed by stunned mice. | [129] |
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Yang, Y.; Hai, Y.; Yang, Y.; Wen, R.; Wang, L.; Qian, Y.; Zhang, J.; Li, Y.; Shi, Z.; Zhang, H. Extraction, Purification, Structural Characteristics, Biological Activities, and Applications of Polysaccharides from Gastrodia elata: A Review. Molecules 2025, 30, 262. https://doi.org/10.3390/molecules30020262
Yang Y, Hai Y, Yang Y, Wen R, Wang L, Qian Y, Zhang J, Li Y, Shi Z, Zhang H. Extraction, Purification, Structural Characteristics, Biological Activities, and Applications of Polysaccharides from Gastrodia elata: A Review. Molecules. 2025; 30(2):262. https://doi.org/10.3390/molecules30020262
Chicago/Turabian StyleYang, Yan, Yonglin Hai, Yongcheng Yang, Rouyuan Wen, Le Wang, Yan Qian, Jiaxian Zhang, Yongguo Li, Zhilong Shi, and Haizhu Zhang. 2025. "Extraction, Purification, Structural Characteristics, Biological Activities, and Applications of Polysaccharides from Gastrodia elata: A Review" Molecules 30, no. 2: 262. https://doi.org/10.3390/molecules30020262
APA StyleYang, Y., Hai, Y., Yang, Y., Wen, R., Wang, L., Qian, Y., Zhang, J., Li, Y., Shi, Z., & Zhang, H. (2025). Extraction, Purification, Structural Characteristics, Biological Activities, and Applications of Polysaccharides from Gastrodia elata: A Review. Molecules, 30(2), 262. https://doi.org/10.3390/molecules30020262