The potential auxiliary effects of Sargassum fusiform polysaccharides on sitagliptin in the treatment of diabetes mellitus.

This work aimed to evaluate the potential positive effects of Sargassum fusiform polysaccharides (SFP) as add-on adjuncts to sitagliptin (SIT) in treating diabetes in rats. The results showed that both SIT and SIT co-administrated with SFP (SIT+SFP) could improve hyperglycemia, glucose tolerance, insulin resistance and hyperlipidemia, and SIT+SFP exhibited better effects in alleviating the levels of blood glucose, glucose tolerance, insulin resistance index, cholesterol, and low-density lipoprotein cholesterol compared to SIT administration. Intestinal flora analysis showed that SIT+SFP treatment significantly restored the beneficial composition of gut flora as compared with SIT administration, such as the increase of Lactobacillus, Romboutsia, Blautia, Bifidobacterium, Bacteroides, Ruminococcaceae_UCG_014 and Ruminococcus_1, and the decrease of Helicobacter, Escherichia-Shigella and Pseudomonas. The fecal metabolite analysis demonstrated that the fecal bile acid and short-chain fatty acid levels in the SIT+SFP group significantly increased compared to SIT treatment. Additionally, mRNA expression results confirmed that the hypoglycemic effects of SIT+SFP were better than those of SIT, which might be attributed to the regulation of blood glucose absorption, inhibition of gluconeogenesis and regulation of cholesterol metabolism. These results suggested that SFP could be used as an auxiliary substance for SIT in treating diabetes mellitus.

Hydrolyzable tannins and pectin are glycolipid lowering ingredients in Phyllanthus emblica Linn.: Valid interaction with gut action targets.

Phyllanthus emblica L., a distinctive fruit, is rich in polyphenols and polysaccharide. However, there is a lack of knowledge regarding the role of these compounds as glycolipid lowering ingredients. In this study, the glycolipid lowering ingredients and their effects have been determined by gradually comparing varieties, parts, and components, splitting components, and calculating combined index via their interactions with digestion enzymes, bile acids, cholesterol micelles and probiotics. Results indicated that the glycolipid lowering ingredients were polyphenols and polysaccharide, which located in the pulp, and not influenced by the variety. Pectin with multiple structural domains, and hydrolyzable tannins, i.e. gallic acid, ellagic acid and their derivatives interacted with multiple gut action targets could regulate glycolipid digestion, absorption and metabolism. Polysaccharide and polyphenols demonstrated a synergistic effect in lowering glycolipid by interacting with gut action targets. These findings highlight the potential for further investigation and utilization of glycolipid lowering ingredients in fruits.

Investigating the impact of static destabilization mechanism on fat crystallization dynamics, emulsion rheology, and whipping properties of whipping cream.

In this work, the effect of storage time on the fat crystallization, rheological and whipping characteristics of emulsions was studied and the static destabilization mechanism during storage was explored. As the storage time prolonged, peak melting temperature and onset of melting temperature increased while both the crystallization temperature and crystallization rate increased. Crystal birefringence was more pronounced at the oil/water interface accompanied by the desorption of interfacial proteins from fat droplets. The droplet size (d4,3) began to increase significantly (p < 0.05) from the 5th month. The viscosity and the elastic modulus increased from 505.2 mPa·s to 908.4 mPa·s, and from 23.53 Pa to 51.38 Pa, respectively, as storing from 1st to 7th month. The whipping time decreased while the partial coalescence rate increased from 50.84 % to 65.34 %. The whipped cream at the 3rd month exhibited a smooth surface, whereas a rough surface and lost gloss was observed at the 7th month.

Mind the Particle Rigidity: Blooms the Bioavailability via Rapidly Crossing the Mucus Layer and Alters the Intracellular Fate of Curcumin.

Overcoming intestinal epithelial barriers to enhance bioavailability is a major challenge for oral delivery systems. Desirable nanocarriers should simultaneously exhibit rapid mucus penetration and efficient epithelial uptake; however, they two generally require contradictory structural properties. Herein, we proposed a strategy to construct multiperformance nanoparticles by modifying the rigidity of amphiphilic nanostructures originating from soy polypeptides (SPNPs), where its ability to overcome multibarriers was examined from both in vitro and in vivo, using curcumin (CUR) as a model cargo. Low-rigidity SPNPs showed higher affinity to mucin and were prone to getting stuck in the mucus layer. When they reached epithelial cells, they tended to be endocytosed through the clathrin and macropinocytosis pathways and further transferred to lysosomes, showing severe degradation and lower transport of CUR. Increased particle rigidity generally improved the absorption of CUR, with medium-rigidity SPNPs bloomed maximum plasma concentration of CUR by 80.62-fold and showed the highest oral bioavailability. Results from monocultured and cocultured cell models demonstrated that medium-rigidity SPNPs were least influenced by the mucus layer and changes in rigidity significantly influenced the endocytosis and intracellular fate of SPNPs. Those with higher rigidity preferred to be endocytosed via a caveolae-mediated pathway and trafficked to the ER and Golgi, facilitating their whole transcytosis, and avoiding intracellular metabolism. Moreover, rigidity modulation efficiently induces the reversible opening of intercellular tight junctions, which synergistically improves the transport of CUR into blood circulation. This study suggested that rigidity regulation on food originated amphiphilic peptides could overcome multiple physiological barriers, showing great potential as natural building block toward oral delivery.

Identification of an arabinogalactan with special structure from Moringa Oleifera leaf and exploration of its immunomodulatory activity.

Arabinogalactan exhibits many biological activities, which is the candidate for functional food ingredients. However, there is limited research on the arabinogalactan from Moringa Oleifera leaf, and its structure needs to be more accurately characterized. This study investigated structural characteristics and immunomodulatory activity of a high-purity polysaccharide from Moringa oleifera leaf (i.e. MOLP-PE) to further explore arabinogalactan from Moringa Oleifera leaf and its potential application area. The results showed that MOLP-PE was a unique type II arabinogalactan: the main chain consisted of → 3, 4)-α-D-Galp-(1→, →3)-ß-D-Galp-(1→ and →2, 4)-ß-D-Rhap-(1→, with branches at the C-4 position of →3, 4)-α-D-Galp-(1→ and →2, 4)-ß-D-Rhap-(1→, consisting of →5)-α-L-Araf-(1→, →3)-α-L-Araf-(1→, →6)-ß-D-Galp-(1→ and →4)-ß-D-GalpA-(1→. Compared with arabinogalactan from larch, galactan and arabinan, MOLP-PE exhibited stronger ability in stimulating proliferation, phagocytosis and cytokines release of macrophages and bound with Toll-like receptor 4 closer via more binding sites, which might be due to its higher contents of 1,3-linked-Galp and 1,5-linked-Araf. These findings elucidated that MOLP-PE, as type II arabinogalactan with a unique structure, could be exploited as an immunomodulatory food ingredient.

Exploring structural features of sleep-enhancing peptides derived from casein hydrolysates by chemometrics and random forest methodology.

Milk casein is regarded as source to release potential sleep-enhancing peptides. Although various casein hydrolysates exhibited sleep-enhancing activity, the underlying reason remains unclear. This study firstly revealed the structural features of potential sleep-enhancing peptides from casein hydrolysates analyzed through peptidomics and multivariate analysis. Additionally, a random forest model and a potential Tyr-based peptide library were established, and then those peptides were quantified to facilitate rapidly-screening. Our findings indicated that YP-, YI/L, and YQ-type peptides with 4-10 amino acids contributed more to higher sleep-enhancing activity of casein hydrolysates, due to their crucial structural features and abundant numbers. Furthermore, three novel strong sleep-enhancing peptides, YQKFPQY, YPFPGPIPN, and YIPIQY were screened, and their activities were validated in vivo. Molecular docking results elucidated the importance of the YP/I/L/Q- structure at the N-terminus of casein peptides in forming crucial hydrogen bond and π-alkyl interactions with His-102 and Asn-60, respectively in the GABAA receptor for activation.

A Comparative Study of the Stability, Transport, and Structure-Activity Relationship of Round Scad Derived Peptides with Antineuroinflammatory Ability.

Our previous study identified round scad neuroprotective peptides with different characteristics. However, the intrinsic relationship between their structure and bioactivity, as well as their bioavailability, remains unclear. The aim of this study is to elucidate the bioavailability of these peptides and their structure-activity relationship against neuroinflammation. Results showed that the SR and WCP peptides were resistant to gastrointestinal digestion. Additionally, peptides SR, WCP, and WCPF could transport Caco-2 monolayers as intact peptides. The permeability coefficients (Papp) of SR, WCP, and WCPF in Caco-2 monolayer were (1.53 ± 0.01) × 10-5, (2.12 ± 0.01) × 10-5, and (8.86 ± 0.03) × 10-7 cm/s, respectively. Peptides SR, WCP, and WCPF, as promising inhibitors of JAK2 and STAT3, could attenuate the levels of pro-inflammatory cytokines and regulate the NFκB and JAK2/STAT3 signaling pathway in LPS-treated BV-2 cells. WCPF exerted the highest anti-inflammatory activity. Moreover, bioinformatics, molecular docking, and quantum chemistry studies indicated that the bioactivity of SR was attributed to Arg, whereas those of WCP and WCPF were attributed to Trp. This study supports the application of round-scad peptides and deepens the understanding of the structure-activity relationship of neuroprotective peptides.

Maintained particulate integrity of soy protein nanoparticles during gastrointestinal digestion via genipin crosslinking enhancing stability and bioavailability of curcumin.

Poor stability during gastrointestinal digestion is a major challenge for the applications of protein-based nanoparticles as oral delivery systems. In this work, genipin was used to crosslink the partially enzymatic hydrolyzed soy protein nanoparticles, aiming to improve their performance in gastrointestinal tract as delivery carrier. Results showed that the obtained genipin-crosslinked soy protein nanoparticles (GSPNPs) were still spherically monodisperse with a diameter around 60 nm. Encapsulation with GSPNPs significantly improved the solubility of curcumin (Cur) and its stability against UV light as well as long-term storage. Compared to those un-crosslinked nanoparticles, particles crosslinked by genipin had a more compact structure less sensitive to ionic effect and digestive enzymes, showing enhanced digestion stability. The well-maintained nanoparticulate structure of GSPNPs further contributed to the enhanced bioaccessibility and facilitated absorption by epithelial cells. Furthermore, in vivo experiment on rats showed that Cur encapsulated in GSPNPs exhibited a slowed down and sustained absorption manner with an 8.11-fold improvement in its bioavailability. These suggested that GSPNPs could be a promising nanocarrier to enhance the bioavailability of functional factors.

Structural characterization and human gut microbiota fermentation in vitro of a polysaccharide from Fucus vesiculosus.

In this study, an acidic polysaccharide (FVP-7 A) was isolated from Fucus vesiculosus by DEAE-Sepharose™ fast flow. The chemical composition, glycosidic bonds and in vitro fecal fermentation characteristics of FVP-7 A were studied. Results shown that FVP-7 A was a homogenous polysaccharide with average molecular weight of 30.94 kDa. Combined with FT-IR, monosaccharide composition, methylation and NMR analysis, the glycosidic bonds of FVP-7 A mainly composed of →4)-ß-D-Manp-(1→, →3)-α-L-Fucp-(1→, α-D-Manp-(1→, →3)-ß-D-Manp-(1 â†’ and →4,6)-α-D-Manp-(1→. The zeta potential and atomic force microscopy images indicated that FVP-7 A could exist stably as a single chain-like structure in dilute solution. After gut fermentation, FVP-7 A was utilized and promoted multiple short-chain fatty acids production, especially acetic acid, butyric acid and valeric acid. For prebiotics, FVP-7 A significantly increased the relative abundance of short-chain fatty acids producing bacteria such as Bacteroides, Lachnospira, Faecalibacterium, Ruminococcus, Oscillospira and Dialister, and inhiited the growth of the harmful bacteria Shigella. These results indicated that FVP-7 A could be used as a potential dietary supplement to improve intestinal health.

Bioactive peptides as a novel strategy to prevent alcoholic liver injury.

Alcohol intake has become one of the leading risks to human health and wellness, among which acute and/or chronic alcohol-induced liver injury is a leading threaten, with few therapeutic options other than abstinence. In recent years, studies suggested that certain bioactive peptides from food sources could represent natural and safe alternatives for the prevention of alcoholic liver injury. Hence, this chapter focus on the advanced research on bioactive peptides exerting hepatoprotective activity against alcoholic liver injury. The main sources of protein, strategies for the preparation of hepatoprotective hydrolysates and peptides, underlying mechanisms of peptides on hepatoprotection, and possible structure-activity relationship between peptides and hepatoprotective activity were summarized and discussed, aiming to give a systematic insight into the research progress of hepatoprotective peptides. However, more efforts would be needed to give a clearer insight into the underlying mechanisms and structure-activity relationship before using hepatoprotective peptides as functional food ingredients or dietary supplements.

Musculus senhousei peptides alleviated alcoholic liver injury via the gut-liver axis.

Alcoholic liver injury has become a leading threat to human health, with complicated pathogenesis and limited therapeutic options. Our previous study showed that Musculus senhousei peptides (MSPs) exhibit protective potential against early-stage alcoholic liver injury, although the underlying mechanism is not yet clear. In this study, histopathological analysis, mRNA abundance of injury-associated biomarkers, the gut microbiota, and faecal metabolome were evaluated using a mouse model subjected to acute alcohol exposure, aiming to identify the mechanism by which MSP can alleviate alcoholic hepatotoxicity. The results showed that MSP intervention significantly ameliorated symptoms of liver injury (suppressed serum ALT increment, hepatic lipid accumulation, and neutrophil infiltration in liver tissue), and reversed the abnormal mRNA abundance of biomarkers associated with oxidative stress (iNOS), inflammation (TNF-α, IL-1ß, MCP-1, TNF-R1, and TLR4), and apoptosis (Bax and Casp. 3) in the liver. Moreover, MSP improved intestinal barrier function by increasing the expression of tight junction proteins (Claudin-1 and Claudin-3). Further analysis of faecal microbiota and metabolome revealed that MSP promoted the growth of tryptophan-metabolizing bacteria (Clostridiales, Alistipes, and Odoribacter), leading to increased production of indole derivatives (indole-3-lactic acid and N-acetyltryptophan). These results suggested that MSPs may alleviate alcohol-induced liver injury targeting the gut-liver axis, and could be an effective option for the prevention of alcoholic liver injury.

Highly Branched Rhamnogalacturonan-I Type Pectin from Wolfberry: Purification, Characterization, and Structure-Prebiotic/Immunomodulatory Activity Relationship.

Due to the difficulty in obtaining highly branched rhamnogalacturonan-I (RG-I) type pectin, the relationship between the extent of RG-I branching (EB) of pectin and prebiotic/immunomodulatory activity has not been systematically investigated. Moreover, it is only possible to establish a structure-activity relationship using pectin that is highly purified and accurately characterized. In this study, a homogeneous highly branched RG-I type pectin (LBP-P4, a final product) with dual proliferative effects on Bifidobacterium and macrophage was effectively purified for the first time using enzyme hydrolysis combined with ultrafiltration. The RG-I content and EB of LBP-P4 reached 97.32 and 77.12, respectively. Its two branches were composed of arabinan and arabinogalactan-II, containing → 5)-Araf-(1→, →3)-Araf-(1→, →3,6)-Galp-(1→ and →6)-Galp-(1→ residues). The structure-activity relationship analysis indicated that strong prebiotic/immunomodulatory activity of LBP-P4 was depended on its high EB, which was further confirmed by the molecular docking simulation between low/high branched pectin with ß-1,6-galactosidase, α-l-arabinanase, and Toll-like receptor 4 (TLR4).

Synthesis, taste characteristics and taste mechanism of N-lactoyl leucine from soy sauce using sensory analysis and UPLC-MS/MS.

Recently, amino acid derivatives gradually gained attention, but studies on N-lactoyl-leucine (Lac-Leu) and N-lactoyl-isoleucine (Lac-Ile) are limited. This study aims to explore the contributions of Lac-Leu and Lac-Ile to soy sauce. Lac-Leu and Lac-Ile were synthesized via enzymatic synthesis method catalyzed by Tgase. The mixed solutions containing Lac-Leu were found to have greater taste improvement than those containing Lac-Ile. Sensory evaluation indicated the sour, bitter, and astringent taste of Lac-Leu in water as well as its kokumi, astringent, and umami-enhancing taste in MSG solution. The taste threshold and umami-enhancing threshold of Lac-Leu measured by TDA and cTDA, respectively, were 0.08 mg/mL and 0.16 mg/mL. Molecular docking of Lac-Leu and Lac-Ile with the kokumi receptor CaSR and the umami receptors T1R1 and T1R3 indicated that Lac-Leu had higher affinities with receptors than Lac-Ile. These findings demonstrated the underlying contribution Lac-Leu made to soy sauce, indicating its potential to improve the flavor quality of soy sauce.

Comparison of the Protective Effects of Casein Hydrolysate Containing Tyr-Pro-Val-Glu-Pro-Phe and Casein on the Behaviors and Peripheral and Brain Functions in Mice with Chronic-Stress-Induced Anxiety and Insomnia.

Chronic stress is a major inducer of anxiety and insomnia. Milk casein has been studied for its stress-relieving effects. We previously prepared a casein hydrolysate (CP) rich in the sleep-enhancing peptide YPVEPF, and this study aims to systemically investigate the different protective effects of CP and casein on dysfunction and anxiety/insomnia behavior and its underlying mechanisms in chronically stressed mice. Behavioral results showed that CP ameliorated stress-induced insomnia and anxiety more effectively than milk casein, and this difference in amelioration was highly correlated with an increase in GABA, 5-HT, GABAA, 5-HT1A receptors, and BDNF and a decrease in IL-6 and NMDA receptors in stressed mice. Furthermore, CP restored these dysfunctions in the brain and colon by activating the HPA response, modulating the ERK/CREB-BDNF-TrκB signaling pathway, and alleviating inflammation. The abundant YPVEPF (1.20 ± 0.04%) and Tyr-based/Trp-containing peptides of CP may be the key reasons for its different effects compared to casein. Thus, this work revealed the main active structures of CP and provided a novel dietary intervention strategy for the prevention and treatment of chronic-stress-induced dysfunction and anxiety/insomnia behaviors.

Enhancing the nonlinear rheological property and digestibility of mung bean flour gels using controlled microwave treatments: Effect of starch debranching and protein denaturation.

In this study, we examined the possibility of using industrial microwave processing to enhance the gelling properties and reduce the starch digestibility of mung bean flour (MBF). MBF (12.6 % moisture) was microwaved at a power of 6 W/g to different final temperatures (100-130 °C), and then its structural and functional properties were characterized. The microwave treatment had little impact on the crystalline structure or amylose content of the starch, but it roughened the starch granule surfaces and decreased the short-range ordered structure and degree of branching. In addition, the extent of mung bean protein denaturation caused by the microwave treatment depended on the final temperature. Slightly denaturing the proteins (100 °C) did not affect the nature of the gels (protein phase dispersed in a starch phase) but the gel network became more compact. Moderately denaturing the proteins (110-120 °C) led to more compact and homogeneous starch-protein double network gels. Excessive protein denaturation (130 °C) caused the gel structure to become more heterogeneous. As a result, the facilitated tangles between starch chains by more linear starch molecules after debranching, and the protein network produced by moderate protein denaturation led to the formation of stronger gel and the improvement of plasticity during large deformation (large amplitude oscillatory shear-LAOS). Starch recrystallization, lipid complexion, and protein network retard starch digestion in the MBF gels. In conclusion, an industrial microwave treatment improved the gelling and digestive properties of MBF, and Lissajous curve has good adaptability in characterizing the viscoelasticity of gels under large deformations.

Molecular Mechanistic Insights into Dipeptidyl Peptidase-IV Inhibitory Peptides to Decipher the Structural Basis of Activity.

Dipeptidyl peptidase-IV (DPP-IV) inhibiting peptides have attracted increased attention because of their possible beneficial effects on glycemic homeostasis. However, the structural basis underpinning their activities has not been well understood. This study combined computational and in vitro investigations to explore the structural basis of DPP-IV inhibitory peptides. We first superimposed the Xaa-Pro-type peptide-like structures from several crystal structures of DPP-IV ligand-protein complexes to analyze the recognition interactions of DPP-IV to peptides. Thereafter, a small set of Xaa-Pro-type peptides was designed to explore the effect of key interactions on inhibitory activity. The intramolecular interaction of Xaa-Pro-type peptides at the first and third positions from the N-terminus was pivotal to their inhibitory activities. Residue interactions between DPP-IV and residues of the peptides at the fourth and fifth positions of the N-terminus contributed significantly to the inhibitory effect of Xaa-Pro-type tetrapeptides and pentapeptides. Based on the interaction descriptors, quantitative structure-activity relationship (QSAR) studies with the DPP-IV inhibitory peptides resulted in valid models with high R2 values (0.90 for tripeptides; 0.91 for tetrapeptides and pentapeptides) and Q2 values (0.33 for tripeptides; 0.68 for tetrapeptides and pentapeptides). Taken together, the structural information on DPP-IV and peptides in this study facilitated the development of novel DPP-IV inhibitory peptides.

Effect of preheating-induced denaturation of proteins and oleosomes on the structure of protein and soymilk properties.

In this paper, effects of preheating-induced denaturation of proteins and oleosomes on protein structure and soymilk quality were studied. The protein in soybeans baked at 55 °C (B-55) and 85 °C (B-85) showed an increase of ß-sheet content by 3.2 % and a decrease of α-helix content by 3.3 %, indicating that proteins were gradually unfolded while oleosomes remained intact. The protein resisted thermal denaturation during secondary heating, and soymilks were stable as reflected by a small d3,2 (0.4 µm). However, raw soymilk from soybeans baked at 115 °C (B-115), steamed for 1 min (ST-1) and 5 min (ST-5) presented oleosomes destruction and lipids aggregates. The proteins were coated around the oil aggregates. The ß-turn content from soybeans steamed for 10 min (ST-10) increased by 9.5 %, with a dense network where the OBs were tightly wrapped, indicating the serious protein denaturation. As a result, the soymilks B-115 or steamed ones were unstable as evidenced by the serious protein aggregation and larger d3,2 (5.65-12.48 µm). Furthermore, the soymilks were graininess and the protein digestion was delayed due to the formation of insoluble protein aggregates. The flavor and early-stage lipid digestion of soymilk from steamed soybeans was improved owing to lipid release.

Effect of fermentation containers on the taste characteristics and microbiota succession of soy sauce.

Modernization of the traditional fermentation industry has been a major trend recently, such as the upgrading of fermentation containers. This study investigated the taste differences and their material basis of soy sauce fermented in tank and pond (SSFT and SSFP), and further explore the key influencing factors of taste. The intensities of umami, kokumi and sour taste in SSFT were weaker than SSFP, which were associated with 9 basic taste-active compounds, including acetic acid, lactic acid, propanedioic acid, citric acid, glutamic acid, alanine, tyrosine, d-galactose and erythritol. Moreover, 270 peptides and amino acid derivatives were potential compounds for taste difference, of which 78 % were more abundant in SSFP. Five bacterial genera (Kocuria, Tetragenococcus, Pediococcus, Staphylococcus, Weissella) and 4 fungal genera (Wickerhamiella, Millerozyma, Candida, Zygosaccharomyces) may be the functional core microbe for flavor differences in SSFT and SSFP. This study will provide theoretical value for quality improvement in the modern large-scale production of soy sauce.

Exploration of green preparation strategy for Lycium barbarum polysaccharide targeting Bacteroides proliferative and immune-enhancing activities and its potential use in geriatric foods.

Lycium barbarum polysaccharide (LBP) is beneficial for elderly people, but its use is limited in geriatric foods due to the lack of comprehensive information on its preparation strategy and physical property. In this study, the low-ester rhamnogalacturonan-I (RG-I) type pectic polysaccharide-protein complexes with varying physicochemical properties, structural characteristics, proliferative activities on Bacteroides, and immune-enhancing activities on RAW 264.7 cells, were obtained by moderate-temperature acid extraction within adjustment of enzymatic and physical pretreatments. LBP prepared by moderate-temperature acid extraction, namely S1-A, showed the strongest immune-enhancing activity via increasing the phagocytosis capacity and NO release of RAW 264.7 cells by 23 % and 76 %, respectively. S1-A exhibited relatively high viscosity and calcium ion response characteristic with the application potential for thickened liquid foods for the elderly with dysphagia. LBP prepared by composite cellulase and pectinase pretreatment combined with moderate-temperature acid extraction, namely S1-M1, showed the strongest Bacteroides proliferative activity that was equivalent to 0.60-0.97 times of that of inulin. S1-M1 exhibited extremely low viscosity and strong tolerance to food nutrients with high processing applicability for fluid foods. This study provided crucial data for the preparation and application of LBP targeting gut microbiota disorders and immunosenescence for the development of geriatric foods.

Simultaneously efficient dissolution and structural modification of chrysanthemum pectin: Targeting at proliferation of Bacteroides.

Pectic polysaccharide is a bioactive ingredient in Chrysanthemum morifolium Ramat. 'Hangbaiju' (CMH), but the high proportion of HG domain limited its use as a prebiotic. In this study, hot water, cellulase-assisted, medium-temperature alkali, and deep eutectic solvent extraction strategies were firstly used to extract pectin from CMH (CMHP). CMHP obtained by cellulase-assisted extraction had high purity and strong ability to promote the proliferation of Bacteroides and mixed probiotics. However, 4 extraction strategies led to general high proportion of HG domain in CMHPs. To further enhance the dissolution and prebiotic potential of CMHP, pectinase was used alone and combined with cellulase. The key factor for the optimal extraction was enzymolysis by cellulase and pectinase in a mass ratio of 3:1 at 1 % (w/w) dosage. The optimal CMHP had high yield (15.15 %), high content of total sugar, and Bacteroides proliferative activity superior to inulin, which was probably due to the cooperation of complex enzyme on the destruction of cell wall and pectin structural modification for raised RG-I domain (80.30 %) with relatively high degree of branching and moderate HG domain. This study provided a green strategy for extraction of RG-I enriched prebiotic pectin from plants.