Yeast β-Glucan - Bioactives with Immune-modulatory properties.: Comparison
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Please note this is a comparison between Version 2 by Peter Tang and Version 1 by Emma J. Murphy.

β-glucans are a large class of complex polysaccharides with bioactive properties, including immune modulation. Natural sources of these compounds include yeast, oats, barley, mushrooms, and algae. Yeast is abundant in various processes, including fermentation, and they are often discarded as waste products. The production of biomolecules from waste resources is a growing trend worldwide with novel waste resources being constantly identified. Yeast-derived β-glucans may assist the host’s defence against infections by influencing neutrophil and macrophage inflammatory and antibacterial activities. β-glucans were long regarded as an essential anti-cancer therapy and were licensed in Japan as immune-adjuvant therapy for cancer in 1980 and new mechanisms of action of these molecules are constantly emerging.

  • β-glucans
  • yeast
  • bioactive properties
  • anti-cancer
  • immune-modulation

1. Introduction

Bioactives such as β-glucans have anti-cancer, anti-inflammatory, and immunomodulatory properties [1,2,3,4][1][2][3][4]. Sources of β-glucans are diverse but can be initially divided into cereal sources, including oat and barley, and non-cereal sources, such as mushrooms, yeast, algae, and bacteria [5]. Classification of β-glucans is essential, as origin dictates structure, which greatly influences biological activity. Firstly, all β-glucans are homo-polysaccharides composed of glucose units [6,7][6][7]. Secondly, they all possess a 1,3 linked backbone fundamental to their activity [8].
Structural contrasts occur in the branching off the 1,3 backbone; the molecule can be branched at various locations and can also be non-branched [9]. Cereal-derived β-glucans have a very different branching structure than non-cereal-derived. There are also inter-source variations. Branching at the 1,4 position is characteristic of cereal derived β-glucans, whereas branching at the 1,6 position is characteristic of non-cereal derived β-glucans [10,11][10][11]. β-glucans, usually from non-cereal sources, can also contain no branching, such as Curdlan, isolated from Agrobacterium [12].
Cereal derived β-glucans have a primarily metabolic effect, including the modulation of the gut microbiome and cholesterol reduction, reducing cardiovascular issues. Non-cereal-derived β-glucans elicit their effects usually through interaction with the immune system. Therapeutic effects include anti-inflammatory, anti-cancer, and anti-infective properties [5]. Recognition by immune cells is not exclusively linked to branching but to the length of the polysaccharide polymer and its tertiary structure as well [8,13][8][13].
Other influences on final conformational structure aside from the originating source include extraction procedure and growth or culture conditions [14]. Herein lies the hurdle of the clinical translation of β-glucans. There are substantial structural variances between β- glucans, including those originating from the same source. These variances include the chain length of the backbone and branching, type of branching, and 3D conformational structure, which can display a random, single helix, or triple helical structure [15]. Thus, research groups are reporting differences in activity which can be seen in an abundance of in-vitro and in-vivo tests and clinical trials registered for the use of β-glucans. β-glucans have been extensively studied in infectious illnesses and tumour immunology.
Yeast cells are an abundant source of β-glucans and are well documented for their biological activity in both humans and animals [5,16][5][16]. Saccharomyces cerevisiae (S. cerevisiae), or baker’s yeasts, are the most often utilised in winemaking and brewing [17,18,19][17][18][19]. Usually, β-glucans are found in residues and byproducts from these applications. One-third to one-half of the yeast’s cell wall is made up of β 1,3-glucan, whereas β 1,6-glucan makes up 10% to 15% of the polysaccharide in the cell wall [20]. This branched structure is a known bioactive that is often discarded as a waste byproduct.

2. Yeast as a Source of β-Glucans

Yeasts are unicellular fungi that reproduce asexually through budding or fission and sexually through spore formation. Currently, 500 yeast species are recognised. The most often used yeasts are S. cerevisiae, which are used in winemaking and brewing [17] and the creation of a variety of nutraceutical goods [18,21][18][21]. Most commercially available hormones are produced using recombinant S. cerevisiae. Insulin and glucagon are two of these hormones [22]. S. cerevisiae has a thick cell wall made up of polysaccharides and proteins which protects the inner compartments of the cell [23,24][23][24]. Up to 55% of the cell wall is composed of β-glucans of 1,3 linkage and 12% of 1,6 β-glucans [23,24][23][24]. Yeast-derived β-glucans contain a linear backbone of (1,3)-linked D-glucose molecules with (1–6) side chains of various lengths. In yeast β-glucans, synthesis can occur in various cell regions. The formation initially occurs in the plasma membrane and is then catalysed enzymatically. The enzyme involved in β-glucan synthesis is β-glucan synthase, encoded by the FKS1 and FKS2 genes [25]. The synthase linked to the cell membrane of S. cerevisiae employs UDP-glucose as a substrate [26,27][26][27]. S. cerevisiae is an industrial microorganism used for protein, chemical, and metabolite synthesis. The unicellular eukaryote is one of the most researched and utilised industrial microorganisms. It is used to make numerous industrial compounds and heterologous proteins in addition to alcohol fermentation, baking, and bio-ethanol processes [28]. Beer production can generate important byproducts in the form of spent brewer’s yeasts which contains β-glucans [29].

3. Production of Yeast β-Glucans from Waste Streams

Biotechnological and commercial interest in the manufacture of yeast is continuing to grow for applications including food, livestock feed, medicinal, cosmetic, and wastewater treatment applications [30]. Numerous cultivation variables, such as the type and availability of carbon and nitrogen sources, the cultivation temperature, pH, degree of aeration, osmotic pressure, time of incubation and growth phase, and mode of yeast propagation all affect the content and characteristics of structural polymers in the yeast cell wall [31,32,33][31][32][33]. The polymerisation of yeast β-glucans depends on external factors, including the growth phase and carbon source [34]. The chemical structure and concentration of the polysaccharide are also determined by the species’ genetic profile [35]. Thus, yeast β-glucans have a variety of lengths, which may be quantified analytically. Conventional chemical characterisation techniques include Fourier transform infrared (FT-IR) and Nuclear magnetic resonance (1HNMR) which determine the structure of a molecule [36]. The characterisation is vital as the chemical structure and function will all have effects on the immune counterpart interaction. Yeast may be quickly grown in a variety of different growth conditions. The biomass of food-grade yeasts is chiefly produced using traditional substrates such as molasses, a byproduct of the sugar industry. Additionally, starch, distiller’s wash, whey, fruit and vegetable wastes, and unusual materials such as petroleum byproducts can also be used [37]. Although yeast β-glucans are usually produced in laboratories using biotechnological processes, they can also be sourced as byproducts from industrial processes. The environmental impact of industrial wastes derived from food sources is a challenge, reuse and disposal options are continuously being researched and tested. Byproducts of the food sector, potato juice and glycerol are two examples, are rich in nutrients and can be used as a digestate for microorganisms through recycling. Potato juice and glycerol are byproducts of the manufacturing of potato starch and biodiesel, respectively [38,39][38][39]. These two byproducts were utilised in research by Bzducha-Wróbel et al. (2015) to develop yeast, alter the cell wall structure, and acquire yeast biomass, eventually increasing the amounts of (1,3)/(1,6)-glucans. Interestingly, the Y.B.D medium, deproteinated potato juice, and 5–10% glycerol as a carbon source enhanced β-glucans synthesis from 31% to 44% [40]. Chotigavin et al. (2021) studied the effects of tannic acid on Saccharomyces carlsbergensis, a brewer’s yeast. Beer fermentation produces a lot of waste. Tannins are utilised in brewing while mashing the hot wort. Tannins interact with the yeast cell wall to form polysaccharides and cause stress in yeast cells which is counteracted by a buildup of β-glucans in the cell wall. Tannic acid increases the thickness of the β-glucan-chitin layer while decreasing the mannoprotein layer. Thicker cell walls correspond with higher carbohydrate and β-glucan levels. The addition of 0.1% w/v tannic acid boosted β-glucan synthesis and content by 42.23%. The stirred tank culture produced 1.4 times more β-glucans than the shaking flask culture [41,42,43][41][42][43]. A novel source for the commercial synthesis of yeast β-glucans was investigated by Varelas et al. (2016). The group isolated β-glucans for the first time from winery spent yeast biomass. During the winemaking process, a byproduct known as wine lees is produced. Most byproducts include spent yeasts, bacteria, tartaric acid, ethanol, phenolics, and pigments. Thus, β-glucans can be sourced from the yeast waste biomass that accumulates in wine tanks throughout the winemaking process. This study showed that the isolated β-glucans contained some amount of tartaric acid and polyphenols, which could not be omitted. Considering wine lees, especially red ones, are more complex mixes than brewery wastes, the purity of β-glucans in wine lees samples was lower than the purity reported by other studies from brewery wastes [44]. Nonetheless, this work identifies a valuable waste source of β-glucans that are most often disposed of in landfills. The structure and content of molasses yeast β-glucans were investigated using High-Performance Liquid Chromatography (HPLC) and NMR [45]. In addition, the effects of β-glucans on the Abelson leukaemia virus-transformed monocyte/macrophage cell line (RAW 264.7) challenged with LPS were investigated. The product yield was reduced due to the yeast cell state. Compared to freshly produced yeast in the laboratory, the yeast waste material was damaged and partially deactivated before extraction. The β-glucan sample demonstrated very effective immune-modulating properties. The extract significantly suppressed TNF-α compared to the positive control and considerably reduced IL-6 production [45].

4. Pathogen Associated Molecular Pattern Recognition

Immune system effectiveness is crucial for eradicating pathogens rapidly and successfully. The immune system is broadly divided into innate or nonspecific immunity and acquired or specific immunity. Innate immunity is the initial line of defence against nonspecific invaders and is instantaneous. Monocytes, macrophages, dendritic cells, and neutrophils are all included in the innate system. Acquired immunity is a more gradual response that occurs after the initial contact and is dependent on B-cells and T-cells. Following the first exposure, the secondary reaction is swift. Both innate and adaptive immune cells are interdependent. Immune cells recognise β-glucans as foreign material or pathogen-associated molecular patterns (PAMPs) as they are prevalent in microbial cell walls. Microbial-based PAMPs are also known as MAMPs. Pathogen recognition receptors on immune cells and mucosal membranes identify and bind these patterns (P.R.R.s) [46]. To exert their biological effects, immune cells must identify β-glucans via P.R.R.s. C-type lectin receptors (CLRs) detect fungal signals [47].

β-Glucan Induction of Trained Immunity

4.1. β-Glucan Induction of Trained Immunity

Initially, it was believed that innate immune cells behaved randomly and lacked the potential for immunological memory. The trained immunity hypothesis implies that innate immune cells respond more effectively and rapidly to viral and microbial infections before sensitisation with specific microbial components (including yeast-derived β-glucans). It has been claimed that stimulants such as β-glucans can induce it [48[48][49][50],49,50], as a result, when these cells are exposed to β-glucans, they build a “memory” which improves their capacity to fight infection [51,52][51][52]. Administration of β-glucans primes the immune response to recognise future microbial insults. The induction of trained immunity is a potential technique for defending against bacterial and viral illnesses. This is achieved by epigenetic reprogramming in innate immune cells, resulting in increased cytokine production and metabolic alterations that shift the cell’s metabolism away from oxidative phosphorylation and glucose fermentation. When these epigenetically “trained” cells encounter secondary stimuli, they are programmed to respond more robustly to those stimuli [53]. Studies suggest that β-glucans can be used in vaccinations as adjuvants. This is because β-glucans activate and modify all parts of the immune system because they induce long-lasting, effective immunity that is widely protective, thus increasing antigen recognition [54].

5. Recognition Receptors for β-Glucans

Dectin-1 is often referred to as the β-glucan receptor. Dectin-1 is expressed on monocytes, macrophages, neutrophils, dendritic cells, and T lymphocytes, activated by the binding of β-glucans [55,56][55][56]. The receptor is also present in mucosal immune cells where pathogens invade. By regulating the inflammasome and transcription factor activation, this binding generates cytokines, chemokines, and reactive oxygen species (ROS) [46,57,58][46][57][58]. This recognition relies on the 1,3 backbone [59]. Several other receptors react to β-glucans, including lactosylceramide, scavenger, and Toll-like receptors [55,60][55][60]. Toll-like receptor (TLR2) binding causes ROS, pro-inflammatory indicators, and pathogen clearance phagocytosis [61]. The pathway activated after binding can either stimulate the immune response and initiate a cascade of inflammatory mediators or, in contrast, dampen down inflammation through modulatory processes [16]. When β-glucans bind to Dectin-1, it increases phosphorylation of its intracellular immunoreceptor tyrosine-based activation motif (ITAM) and Syk and activates the PI3K/Akt pathway. This finally results in phagocytosis, the creation of ROS, microbial death, and cytokine release [62,63,64][62][63][64]. A more detailed graphical representation of this process can be found at [65,66][65][66]. Neutrophils, monocytes, and natural killer (NK) cells express the CR3 receptor. CR3 is distinctive in that it contains two different binding sites for ligands. A carbohydrate-binding lectin-like domain, which can bind β-glucans, serves as the second ligand-binding site. Binding will enhance cytotoxicity against iC3b-opsonized target cells such as tumour cells, phagocytosis, and degranulation [67]. The CR3 produced by innate cells such as macrophages, dendritic cells, natural killer cells, and neutrophils binds to yeast-derived low molecular weight soluble β-glucans. The CR3 receptor is activated by the binding of soluble β-glucans and iC3b, and this leads to the destruction of tumour cells coated with iC3b through CR3-dependent cellular cytotoxicity (DCC) [68].

6. Yeast β-Glucan Administration to Humans

Yeast β-glucans’ are currently registered for a range of clinical trials on clinicaltrials.gov (accessed on 28 March 2022) as outlined in Table 1. In terms of administration, oral glucan has been investigated the most, but intravenous and intraperitoneal glucan injections have also been employed. Oral glucans are phagocytosed by intestinal epithelial cells or pinocytic microfold cells (M-cells), which transfer glucan from the intestinal lumen to immune cells within Peyer’s patches [13,69][13][69]. Conversely, in humans, researchers found no changes in cytokine production or the microbicidal activity of leukocytes after seven days of oral glucan ingestion, and no glucan itself in volunteers’ serum [70]. They are also administered for different interventions. The immune-modulatory properties and anti-cancer properties dominate the majority of studies carried out.
Table 1. Registered clinical trials on yeast β-glucan as a potential therapeutic agent. Information from clinicaltrials.gov (accessed on 28 March 2022). * n/a; information not available.

Clinical Trial Number

Title

Yeast β-Glucan Dose

Disease

Phase

NCT03495362

The Effect of Insoluble yeast Beta-glucan Intake on Pre-diabetic Patients

Oral administration of 500 mg insoluble β-glucan twice a day

Pre-diabetic

n/a *

NCT05074303

Beta-glucan and Immune Response to Influenza Vaccine (M-Unity)

Oral administration of 500 mg/day

Influenza Vaccine

Phase I

NCT00492167

Beta-Glucan and Monoclonal Antibody 3F8 in Treating Patients with Metastatic Neuroblastoma

Oral administration Dose escalation

Neuroblastoma

Phase I

NCT01829373

Lung Cancer Vaccine Plus Oral Dietary Supplement

Oral administration

Lung Cancer

Phase I

NCT01727895

Effects of Orally Administered Beta-glucan on Leukocyte Function in Humans (BG)

Oral administration of 2 capsules of 500 mg/Daily

Immunologic Deficiency Syndromes

n/a

NCT04798677

Efficacy and Tolerability of ABBC1 in Volunteers Receiving the Influenza or COVID-19 Vaccine

Oral administration Powder for dissolution in water

Immunity

Vaccine Reaction

Influenza

COVID-19

Cytokine Storm

Immunologic Deficiency Syndromes

n/a

NCT03782974

A Follow-up Trial of Proglucamune® in the Treatment of Protective Qi Insufficiency, a T.C.M. Condition

Oral administration of 100 mg/day

Protective Qi Insufficiency (a Condition Term from T.C.M.)

n/a

NCT04710290

A Cohort Study of Beta-Glucan or Beta-Glucan Compound in Metastatic Cancers

Oral administration of beverage powder or capsule

Metastatic Cancer

Phase II

Phase III

NCT01910597

Phase I, Dose-Escalation Study of Soluble Beta-Glucan (S.B.G.) in Patients with Advanced Solid Tumours

n/a

Advanced Solid Tumours

Phase 1

NCT04301609

Clinical Trial to Assess the Improvement of Fatigue, Sleep Problems, Anxiety/Depression, Neurovegetatives Alterations, and Quality of Life After the Administration of ImmunoVita® in Chronic Fatigue Syndrome Patients

Oral Administration

Chronic Fatigue SyndromeMyalgic Encephalomyelitis

n/a

NCT04387682

Myeloid-derived Suppressor Cells (MDSCs) in OSCC Patients

Dietary Supplementation

Squamous Cell Carcinoma of the Oral Cavity

n/a

NCT03717714

Polycan in Combination with Glucosamine for Treatment of Knee Osteoarthritis

Oral Administration of 50 mg/day

Osteoarthritis of the Knee

n/a

NCT01402115

A 12-week Human Trial to Compare the Efficacy and Safety of Polycan on Bone Metabolism

Dietary Supplementation

Bone Health in Perimenopausal Women

Phase II

Phase III

NCT04810572

Nutraceutical Composition Containing Natural Products Derivatives on the Modulation of the Endocrine Neuroimmune Axis (NCCNPDMENA)

Dietary Supplementation

Insulin Resistance Inflammatory Bowel Diseases

Obesity

Healthy

n/a

NCT00911560

Bivalent Vaccine with Escalating Doses of the Immunological Adjuvant OPT-821, in Combination With Oral β-glucan for High-Risk Neuroblastoma

Oral Administration

of 40 mg/kg/day

Neuroblastoma

Phase II

Phase III

References

  1. Zabriskie, H.A.; Blumkaitis, J.C.; Moon, J.M.; Currier, B.S.; Stefan, R.; Ratliff, K.; Harty, P.S.; Stecker, R.A.; Rudnicka, K.; Jäger, R.; et al. Yeast Beta-Glucan Supplementation Downregulates Markers of Systemic Inflammation after Heated Treadmill Exercise. Nutrients 2020, 12, 1144.
  2. Wang, N.; Liu, H.; Liu, G.; Li, M.; He, X.; Yin, C.; Tu, Q.; Shen, X.; Bai, W.; Wang, Q.; et al. Yeast β-D-Glucan Exerts Antitumour Activity in Liver Cancer through Impairing Autophagy and Lysosomal Function, Promoting Reactive Oxygen Species Production and Apoptosis. Redox Biol. 2020, 32, 101495.
  3. Fuller, R.; Butt, H.; Noakes, P.S.; Kenyon, J.; Yam, T.S.; Calder, P.C. Influence of Yeast-Derived 1,3/1,6 Glucopolysaccharide on Circulating Cytokines and Chemokines with Respect to Upper Respiratory Tract Infections. Nutrition 2012, 28, 665–669.
  4. Dharsono, T.; Rudnicka, K.; Wilhelm, M.; Schoen, C. Effects of Yeast (1,3)-(1,6)-Beta-Glucan on Severity of Upper Respiratory Tract Infections: A Double-Blind, Randomized, Placebo-Controlled Study in Healthy Subjects. J. Am. Coll. Nutr. 2019, 38, 40–50.
  5. Murphy, E.J.; Rezoagli, E.; Major, I.; Rowan, N.J.; Laffey, J.G. Β-Glucan Metabolic and Immunomodulatory Properties and Potential for Clinical Application. J. Fungi 2020, 6, 356.
  6. Zhang, H.; Zhang, N.; Xiong, Z.; Wang, G.; Xia, Y.; Lai, P.; Ai, L. Structural Characterization and Rheological Properties of β-D-Glucan from Hull-Less Barley (Hordeum vulgare L. Var. Nudum Hook. f.). Phytochemistry 2018, 155, 155–163.
  7. Friedman, M. Mushroom Polysaccharides: Chemistry and Antiobesity, Antidiabetes, Anticancer, and Antibiotic Properties in Cells, Rodents, and Humans. Foods 2016, 5, 80.
  8. Han, B.; Baruah, K.; Cox, E.; Vanrompay, D.; Bossier, P. Structure-Functional Activity Relationship of β-Glucans From the Perspective of Immunomodulation: A Mini-Review. Front. Immunol. 2020, 11, 658.
  9. Kaur, R.; Sharma, M.; Ji, D.; Xu, M.; Agyei, D. Structural Features, Modification, and Functionalities of Beta-Glucan. Fibers 2020, 8, 1.
  10. Jin, Y.; Li, P.; Wang, F. β-Glucans as Potential Immunoadjuvants: A Review on the Adjuvanticity, Structure-Activity Relationship and Receptor Recognition Properties. Vaccine 2018, 36, 5235–5244.
  11. Du, B.; Meenu, M.; Liu, H.; Xu, B. A Concise Review on the Molecular Structure and Function Relationship of β-Glucan. Int. J. Mol. Sci. 2019, 20, 4032.
  12. Zhan, X.B.; Lin, C.C.; Zhang, H.T. Recent Advances in Curdlan Biosynthesis, Biotechnological Production, and Applications. Appl. Microbiol. Biotechnol. 2012, 93, 525–531.
  13. Stier, H.; Ebbeskotte, V.; Gruenwald, J. Immune-Modulatory Effects of Dietary Yeast Beta-1,3/1,6-D-Glucan. Nutr. J. 2014, 13, 38.
  14. Murphy, E.J.; Rezoagli, E.; Major, I.; Rowan, N.; Laffey, J.G. β-Glucans. Encyclopedia 2021, 10, 64.
  15. Wang, Q.; Sheng, X.; Shi, A.; Hu, H.; Yang, Y.; Liu, L.; Fei, L.; Liu, H. β-Glucans: Relationships between Modification, Conformation and Functional Activities. Molecules 2017, 22, 257.
  16. Murphy, E.J.; Rezoagli, E.; Pogue, R.; Simonassi-Paiva, B.; Abidin, I.I.Z.; Fehrenbach, G.W.; O’Neil, E.; Major, I.; Laffey, J.G.; Rowan, N. Immunomodulatory Activity of β-Glucan Polysaccharides Isolated from Different Species of Mushroom—A Potential Treatment for Inflammatory Lung Conditions. Sci. Total Environ. 2022, 809, 152177.
  17. Joseph, R.; Bachhawat, A.K. Yeasts: Production and Commercial Uses. In Encyclopedia of Food Microbiology, 2nd ed.; Academic Press: Cambridge, MA, USA, 2014; pp. 823–830.
  18. Padilla, B.; Frau, F.; Ruiz-Matute, A.I.; Montilla, A.; Belloch, C.; Manzanares, P.; Corzo, N. Production of Lactulose Oligosaccharides by Isomerisation of Transgalactosylated Cheese Whey Permeate Obtained by β-Galactosidases from Dairy Kluyveromyces. J. Dairy Res. 2015, 82, 356–364.
  19. Jeyaram, K.; Rai, A.K. Role of Yeasts in Food Fermentation. In Yeast Diversity in Human Welfare; Springer: Singapore, 2017; pp. 83–113.
  20. Suzuki, T.; Nishikawa, K.; Nakamura, S.; Suzuki, T. Research and Development of β-1,3-1,6-Glucan from Black Yeast for a Functional Food Ingredient. Bull. Appl. Glycosci. 2012, 2, 51–60.
  21. Rai, A.K.; Sanjukta, S.; Jeyaram, K. Production of Angiotensin I Converting Enzyme Inhibitory (ACE-I) Peptides during Milk Fermentation and Their Role in Reducing Hypertension. Crit. Rev. Food Sci. Nutr. 2017, 57, 2789–2800.
  22. Walsh, G. Biopharmaceutical Benchmarks 2018. Nat. Biotechnol. 2018, 36, 1136–1145.
  23. Varelas, V.; Liouni, M.; Calokerinos, A.C.; Nerantzis, E.T. An Evaluation Study of Different Methods for the Production of β-D-Glucan from Yeast Biomass. Drug Test. Anal. 2016, 8, 46–55.
  24. Wang, J.; Li, M.; Zheng, F.; Niu, C.; Liu, C.; Li, Q.; Sun, J. Cell Wall Polysaccharides: Before and after Autolysis of Brewer’s Yeast. World J. Microbiol. Biotechnol. 2018, 34, 137.
  25. Aimanianda, V. Transglycosidases and Fungal Cell Wall β-(1,3)-Glucan Branching. Mol. Biol. 2017, 6, 3.
  26. Kasahara, S.; Yamada, H.; Mio, T.; Shiratori, Y.; Miyamoto, C.; Yabe, T.; Nakajima, T.; Ichishima, E.; Furuichi, Y. Cloning of the Saccharomyces cerevisiae Gene Whose Overexpression Overcomes the Effects of HM-1 Killer Toxin, Which Inhibits β-Glucan Synthesis. J. Bacteriol. 1994, 176, 1488–1499.
  27. Tartar, A.; Shapiro, A.M.; Scharf, D.W.; Boucias, D.G. Differential Expression of Chitin Synthase (CHS) and Glucan Synthase (FKS) Genes Correlates with the Formation of a Modified, Thinner Cell Wall in in Vivo-Produced Beauveria Bassiana Cells. Mycopathologia 2005, 160, 303–314.
  28. Mattanovich, D.; Sauer, M.; Gasser, B. Yeast Biotechnology: Teaching the Old Dog New Tricks. Microb. Cell Factories 2014, 13, 34.
  29. San Martin, D.; Orive, M.; Iñarra, B.; Castelo, J.; Estévez, A.; Nazzaro, J.; Iloro, I.; Elortza, F.; Zufía, J. Brewers’ Spent Yeast and Grain Protein Hydrolysates as Second-Generation Feedstuff for Aquaculture Feed. Waste Biomass Valorization 2020, 11, 5307–5320.
  30. Zhu, F.; Du, B.; Xu, B. A Critical Review on Production and Industrial Applications of Beta-Glucans. Food Hydrocoll. 2016, 52, 275–288.
  31. Aguilar-Uscanga, B.; François, J.M. A Study of the Yeast Cell Wall Composition and Structure in Response to Growth Conditions and Mode of Cultivation. Lett. Appl. Microbiol. 2003, 37, 268–274.
  32. Naruemon, M.; Romanee, S.; Cheunjit, P.; Xiao, H.; Mclandsborough, L.A.; Pawadee, M. Influence of Additives on Saccharomyces cerevisiae β-Glucan Production. Int. Food Res. J. 2013, 20, 1953–1959.
  33. Bzducha-Wróbel, A.; Błazejak, S.; Tkacz, K. Cell Wall Structure of Selected Yeast Species as a Factor of Magnesium Binding Ability. Eur. Food Res. Technol. 2012, 235, 355–366.
  34. Avramia, I.; Amariei, S. Spent Brewer’s Yeast as a Source of Insoluble β-Glucans. Int. J. Mol. Sci. 2021, 22, 825.
  35. Gow, N.A.R.; Latge, J.-P.; Munro, C.A. The Fungal Cell Wall: Structure, Biosynthesis, and Function. Microbiol. Spectr. 2017, 5, 267–292.
  36. Gonzaga, M.L.C.; Menezes, T.M.F.; de Souza, J.R.R.; Ricardo, N.M.P.S.; Soares, S.D.A. Structural Characterization of β Glucans Isolated from Agaricus Blazei Murill Using NMR and FTIR Spectroscopy. Bioact. Carbohydr. Diet. Fibre 2013, 2, 152–156.
  37. Bzducha-Wróbel, A.; Pobiega, K.; Błażejak, S.; Kieliszek, M. The Scale-up Cultivation of Candida Utilis in Waste Potato Juice Water with Glycerol Affects Biomass and β(1,3)/(1,6)-Glucan Characteristic and Yield. Appl. Microbiol. Biotechnol. 2018, 102, 9131–9145.
  38. Binhayeeding, N.; Klomklao, S.; Sangkharak, K. Utilization of Waste Glycerol from Biodiesel Process as a Substrate for Mono-, Di-, and Triacylglycerol Production. Energy Procedia 2017, 138, 895–900.
  39. Ciecholewska-juśko, D.; Broda, M.; Żywicka, A.; Styburski, D.; Sobolewski, P.; Gorący, K.; Migdał, P.; Junka, A.; Fijałkowski, K. Potato Juice, a Starch Industry Waste, as a Cost-Effective Medium for the Biosynthesis of Bacterial Cellulose. Int. J. Mol. Sci. 2021, 22, 10807.
  40. Bzducha-Wróbel, A.; Błażejak, S.; Molenda, M.; Reczek, L. Biosynthesis of β(1,3)/(1,6)-Glucans of Cell Wall of the Yeast Candida Utilis ATCC 9950 Strains in the Culture Media Supplemented with Deproteinated Potato Juice Water and Glycerol. Eur. Food Res. Technol. 2015, 240, 1023–1034.
  41. Chotigavin, N.; Sriphochanart, W.; Yaiyen, S.; Kudan, S. Increasing the Production of β-Glucan from Saccharomyces Carlsbergensis RU01 by Using Tannic Acid. Appl. Biochem. Biotechnol. 2021, 193, 2591–2601.
  42. Fumi, M.D.; Galli, R.; Lambri, M.; Donadini, G.; de Faveri, D.M. Effect of Full-Scale Brewing Process on Polyphenols in Italian All-Malt and Maize Adjunct Lager Beers. J. Food Compos. Anal. 2011, 24, 568–573.
  43. Zhang, W.; Tang, Y.; Liu, J.; Jiang, L.; Huang, W.; Huo, F.W.; Tian, D. Colorimetric Assay for Heterogeneous-Catalyzed Lipase Activity: Enzyme-Regulated Gold Nanoparticle Aggregation. J. Agric. Food Chem. 2015, 63, 39–42.
  44. Varelas, V.; Tataridis, P.; Liouni, M.; Nerantzis, E.T. Valorization of Winery Spent Yeast Waste Biomass as a New Source for the Production of β-Glucan. Waste Biomass Valorization 2016, 7, 807–817.
  45. Krisdaphong, T.; Toida, T.; Popp, M.; Sichaem, J.; Natkanktkul, S. Evaluation of Immunological and Moisturizing Activities of Beta-Glucan Isolated from Molasses Yeast Waste. Indian J. Pharm. Sci. 2018, 80, 795–801.
  46. Li, D.; Wu, M. Pattern Recognition Receptors in Health and Diseases. Signal Transduct. Target. Ther. 2021, 6, 291.
  47. Tang, J.; Lin, G.; Langdon, W.Y.; Tao, L.; Zhang, J. Regulation of C-Type Lectin Receptor-Mediated Antifungal Immunity. Front. Immunol. 2018, 9, 123.
  48. Arts, R.J.W.; Carvalho, A.; La Rocca, C.; Palma, C.; Rodrigues, F.; Silvestre, R.; Kleinnijenhuis, J.; Lachmandas, E.; Gonçalves, L.G.; Belinha, A.; et al. Immunometabolic Pathways in BCG-Induced Trained Immunity. Cell Rep. 2016, 17, 2562–2571.
  49. McBride, M.A.; Owen, A.M.; Stothers, C.L.; Hernandez, A.; Luan, L.; Burelbach, K.R.; Patil, T.K.; Bohannon, J.K.; Sherwood, E.R.; Patil, N.K. The Metabolic Basis of Immune Dysfunction Following Sepsis and Trauma. Front. Immunol. 2020, 11, 1043.
  50. Zhang, Z.; Chi, H.; Dalmo, R.A. Trained Innate Immunity of Fish Is a Viable Approach in Larval Aquaculture. Front. Immunol. 2019, 10, 42.
  51. Bekkering, S.; Blok, B.A.; Joosten, L.A.B.; Riksen, N.P.; van Crevel, R.; Netea, M.G. In Vitro Experimental Model of Trained Innate Immunity in Human Primary Monocytes. Clin. Vaccine Immunol. 2016, 23, 926–933.
  52. Acevedo, O.A.; Berrios, R.V.; Rodríguez-Guilarte, L.; Lillo-Dapremont, B.; Kalergis, A.M. Molecular and Cellular Mechanisms Modulating Trained Immunity by Various Cell Types in Response to Pathogen Encounter. Front. Immunol. 2021, 12, 4082.
  53. Del Cornò, M.; Gessani, S.; Conti, L. Shaping the Innate Immune Response by Dietary Glucans: Any Role in the Control of Cancer? Cancers 2020, 12, 155.
  54. Petit, J.; Wiegertjes, G.F. Long-Lived Effects of Administering β-Glucans: Indications for Trained Immunity in Fish. Dev. Comp. Immunol. 2016, 64, 93–102.
  55. Kalia, N.; Singh, J.; Kaur, M. The Role of Dectin-1 in Health and Disease. Immunobiology 2021, 226, 152071.
  56. Wagener, M.; Hoving, J.C.; Ndlovu, H.; Marakalala, M.J. Dectin-1-Syk-CARD9 Signaling Pathway in TB Immunity. Front. Immunol. 2018, 9, 225.
  57. Camilli, G.; Bohm, M.; Piffer, A.C.; Lavenir, R.; Williams, D.L.; Neven, B.; Grateau, G.; Georgin-Lavialle, S.; Quintin, J. β-Glucan–Induced Reprogramming of Human Macrophages Inhibits NLRP3 Inflammasome Activation in Cryopyrinopathies. J. Clin. Investig. 2020, 130, 4561–4573.
  58. Canton, M.; Sánchez-Rodríguez, R.; Spera, I.; Venegas, F.C.; Favia, M.; Viola, A.; Castegna, A. Reactive Oxygen Species in Macrophages: Sources and Targets. Front. Immunol. 2021, 12.
  59. Batbayar, S.; Lee, D.H.; Kim, H.W. Immunomodulation of Fungal β-Glucan in Host Defense Signaling by Dectin-1. Biomol. Ther. 2012, 20, 433–445.
  60. Fang, J.; Wang, Y.; Lv, X.; Shen, X.; Ni, X.; Ding, K. Structure of a β-Glucan from Grifola Frondosa and Its Antitumor Effect by Activating Dectin-1/Syk/NF-ΚB Signaling. Glycoconj. J. 2012, 29, 365–377.
  61. Ellefsen, C.F.; Wold, C.W.; Wilkins, A.L.; Rise, F.; Samuelsen, A.B.C. Water-Soluble Polysaccharides from Pleurotus Eryngii Fruiting Bodies, Their Activity and Affinity for Toll-like Receptor 2 and Dectin-1. Carbohydr. Polym. 2021, 264, 117991.
  62. Brown, G.D. Dectin-1 : A Signalling Non-TLR Pattern-Recognition Receptor. Nat. Rev. Immunol. 2006, 6, 33–43.
  63. Brown, G.D.; Herre, J.; Williams, D.L.; Willment, J.A.; Marshall, A.S.J.; Gordon, S. Dectin-1 Mediates the Biological Effects of β-Glucans. J. Exp. Med. 2003, 197, 1119–1124.
  64. Herre, J.; Marshall, A.S.J.; Caron, E.; Edwards, A.D.; Williams, D.L.; Schweighoffer, E.; Tybulewicz, V.; Reis E Sousa, C.; Gordon, S.; Brown, G.D. Dectin-1 Uses Novel Mechanisms for Yeast Phagocytosis in Macrophages. Blood 2004, 104, 4038–4045.
  65. Plato, A.; Hardison, S.E.; Brown, G.D. Pattern Recognition Receptors in Antifungal Immunity. Semin. Immunopathol. 2015, 37, 97–106.
  66. de Castro, R.O. Regulation and Function of Syk Tyrosine Kinase in Mast Cell Signaling and Beyond. J. Signal Transduct. 2011, 2011, 507291.
  67. O’Brien, X.M.; Heflin, K.E.; Lavigne, L.M.; Yu, K.; Kim, M.; Salomon, A.R.; Reichner, J.S. Lectin Site Ligation of CR3 Induces Conformational Changes and Signaling. J. Biol. Chem. 2012, 287, 3337–3348.
  68. Li, B.; Cai, Y.; Qi, C.; Hansen, R.; Ding, C.; Mitchell, T.C.; Yan, J. Orally Administered Particulate β-Glucan Modulates Tumor-Capturing Dendritic Cells and Improves Antitumor t-Cell Responses in Cancer. Clin. Cancer Res. 2010, 16, 5153–5164.
  69. Volman, J.J.; Ramakers, J.D.; Plat, J. Dietary Modulation of Immune Function by β-Glucans. Physiol. Behav. 2008, 94, 276–284.
  70. Leentjens, J.; Quintin, J.; Gerretsen, J.; Kox, M.; Pickkers, P.; Netea, M.G. The Effects of Orally Administered Beta-Glucan on Innate Immune Responses in Humans, a Randomized Open-Label Intervention Pilot-Study. PLoS ONE 2014, 9, e108794.
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