Production of cyclodextrins by microbial CGTases.
Abstract
There is much interest in the study and production of nondigestible oligosaccharides (NDOs), due to their bioactivities and beneficial effects to the human health. The main approach in the production of NDOs relies on the action of glycosidases performing hydrolysis or transglycosylation of polysaccharides and sugars. In this chapter, a description of the main microbial glycosidases used for NDOs production, their sources, their principal properties, and a description of the production processes with the better results obtained are discussed.
Keywords
- glycosidases
- transglysosylation
- enzymatic hydrolysis
- oligosaccharides
1. Introduction
The concept of nondigestible oligosaccharides (NDOs) came from the observation that the human body does not have the necessary enzymes to hydrolyze β-glycosidic linkages present in some sugars of the human diet. Thus, these carbohydrates can arrive intact in the intestine where they are fermented selectively stimulating the growth and/or activity of bacteria in the colon acting as prebiotics [1]. In this context, nondigestible oligosaccharides have received much attention since they have important biological properties promoting health beneficial effects. Stimulation of the intestinal microbiota growth associated with low cariogenic and caloric value are some of these properties. Also noteworthy is a stimulation of the immune system leading to a reduced risk of diarrhea and other infections. The benefits are obtained by a decrease in intestinal pH due to the fermentation of NDOs, decreasing the proliferation of pathogenic microorganisms, and an increase of the bifidobacteria population [2]. The bioactive properties of NDOs can be influenced by monosaccharide composition, type of glycosidic linkage, and degree of polymerization [2].
Nondigestible oligosaccharides can be produced using chemical or enzymatic processes. The synthesis using chemical methods are complicated, with numerous protection and deprotection steps required in order to achieve regioselectivity [3]. Other challenges of chemical synthesis are the low yields, expensive chemicals, and impossibility for scale-up. For those reasons with few exceptions, most of the NDOs are produced by enzymatic processes.
The enzymatic production of NDOs can be achieved by two different approaches, the use of glycosyltransferases or glycosidases. Glycosyltransferases catalyze the stereospecific and regiospecific transfer of a monosaccharide from a donor substrate (glycosyl nucleotide) to an acceptor substrate. Some of the difficulties associated with the application of glycosyltransferases are availability of enzymes and sugar nucleotide donors, product inhibition, and reagent costs. These factors decrease the applications of these enzymes in the production of NDOs [4]. The glycosidases offer a good alternative for enzymatic production of NDOs, where they can be synthetized from monosaccharides using transglycosylation reactions, or formed by controlled enzymatic hydrolysis of polysaccharides. Some advantages of the glycosidases in relation to glycosyltransferases are availability, good stability, and the fact that they act on easily found substrates and do not need cofactors [3].
The transglycosylation route can be performed by the use of a good glycosyl donor that can be a disaccharide, in high concentrations. This donor will form an intermediate glycosyl-enzyme that can be intercepted by an acceptor to give a new glycoside or oligosaccharide [3]. When the substrate is a monosaccharide, it will be acting as a donor and acceptor. Some glycosidases used to produce NDOs using this approach are α-galactosidases, β-fructofuranosidase, cyclomaltodextrin glucanotransferase, and α-glucosidase [4].
The production of NDOs by controlled hydrolysis of polysaccharides involves the break of glycosidic bonds, the reaction is acid base catalyzed by an oxocarbenium ion-like transition state and involves two carboxylic groups at the active site [5]. The glycosidases can be divided into inverting or retaining depending on the configuration of the glycosidic linkage after the hydrolysis. Inverting glycosidases operate through direct displacement of the leaving group by water. The two carboxylic groups are responsible for the reaction, one provides base catalytic assistance to the attack of water and the other provides acid catalytic assistance to cleavage of the glycosidic bond. Retaining glycosidases use a double displacement mechanism involving the formation of a covalent glycosyl enzyme intermediate, where one carboxylic group acts as acid catalyst for the glycosylation step and base catalyst for the deglycosylation step [3]. The second carboxylic group acts as a nucleophile and a leaving group. The enzymes inulinase, pullulanase, amylase, xylanase, endogalactanase, rhamnogalacturonase, endogalacturonase, and chitosanase are used for NDOs production using the controlled hydrolysis approach [4].
2. Production of NDOs through glycosyl transfer reaction
2.1. Galactosidases
β-Galactosidases (EC 3.2.1.23) hydrolyze the nonreducing terminal of β-D-galactose residues in β-D-galactosides. The enzyme can be used in the production of galacto-oligosaccarides (GOs) by transgalactosylation reaction in which a galactosyl is transferred into the hydroxyl group of the galactose residue of lactose [6]. Due to the strong prebiotic factor, GOs can modulate the grown of microorganisms of the gut flora, increasing the population of bifidobacteria, this enhancement is associated with beneficial effects, inhibition the grown of potentially pathogens, improvement, elimination, prevention, stimulation mineral adsorption, and decrement cholesterol and lipids [7].
When using concentrated solutions of lactose (40%), high yields of GOs can be achieved. The β-galactosidase of
The milk whey, a by-product from the dairy industry, is a valuable substrate for GOs productions due to its lactose contend (45–60%). The whey is produced by the processing and manufacturing of raw milk into products such as yogurt, ice cream, butter, and cheese through processes such as pasteurization, coagulation, filtration, centrifugation, chilling, etc. [11]. Depending on the procedure used to precipitate the casein, two types of whey are formed, the acid whey (pH < 5) is obtained after fermentation or addition of organic or mineral acids, whereas the sweet whey (pH 6–7) is obtained by addition of proteolytic enzymes like chymosin [12]. The production of GOs from milk whey using a two-dimensional packed bed bioreactor yielded 97% [13], while a yield of 29.9% of GOs with a concentration of (119.8 mg/mL) was achieved using cheese whey as substrate in a 4 h process [14]. When whey permeate was used as substrate in a membrane reactor system, a mixture of GOs with 77–78% of purity was produced [15]. A high lactose conversion was achieved (70–80%), when using whey as a substrate in the production of GOs, yielding 10–20% of total sugars and producing oligomers with DP3, DP4, and DP5 [16]. The GOs production from whey permeate yielded 50% corresponding to 322 g prebiotics/kg whey permeate, presenting tagatose and lactulose in the oligosaccharides mixture [17]. Galacto-oligosaccharides were synthesized by enzymatic transgalactosylation in UF-skimmed milk permeate fortified with lactose (40% w/w). The GOs yields, expressed as a percentage of the initial lactose content, were 41, 21, 13, and 11% with β-galactosidase from
2.2. β-fructofuranosidases
The β-D-fructofuranosidases catalyze the hydrolysis of β-D-fructofuranoside residues at the nonreducing end of β-D-fructofuranosides [19]. Fructooligosaccharides (FOs) can be produced by transfructosylation of sucrose by β-fructofuranosidases, which is carried out through the breaking of the β(2-1) glycosidic bond and the transfer of the fructosyl moiety onto any acceptor other than water, such as sucrose or a FO. The sucrose is used as substrate acting as the glycosyl donor and as the glycosyl acceptor in competition with water (hydrolysis) in a glycosyl transfer reaction [20]. Besides the strong prebiotic factor, many bioactivities have been associated with FOs as anti-inflammatory effect on Crohn’s disease and ulcerative colitis, antimicrobial activity against gut flora pathogens, and prevention of colon cancer [21].
A β-fructofuranosidase from
2.3. Cyclomaltodextrin glucanotransferase
Cyclomaltodextrin glucanotranferase (CGTase, EC 2.4.1.19) catalyze the cyclization of oligosaccharides composed of D-glucose monomers joined by α(1-4) glycosidic linkages. This enzyme catalyzes mainly transglycosylation reactions leading to the formation of nonreducing cyclic oligosaccharides, named cyclodextrins. The main types are α-, β-, and γ-cyclodextrins consisting of six, seven, and eight glucose monomers in cycles, respectively. The majority of the CGTases usually produce a mixture of α-, β-, and γ-cyclodextrins, and the product ratio can vary depending on condition and reaction time [28].
The CGTase can produce cyclodextrins from starch, amylose, and other polysaccharides by catalyzing different transglycosylation steps: intermolecular coupling and disproportionation and modification of the length of noncyclic dextrins [29]. Between main microbial sources of CGTases, the
The products of the CGTases α, β, and γ-cyclodextrins are not completely digested in the gastrointestinal tract, rising to the colon where they are fermented by the intestinal microflora and for this reason are considered prebiotics. The microbial degradation results in linear malto-oligosaccharides, which are further hydrolyzed and fermented to absorbable and metabolize short-chain fatty acids. Several studies showed that CDs reduce the digestion of starch and the glycemic index of food. Other bioactivities include hypocholesterolemic and antithrombotic activity [30].
The most frequently used raw material for CDs production is starch. The product inhibition effect of cyclodextrins on CGTases, make the complete conversion of starch a challenge. Strategies to decrease this effect involve the continual removal of CDs by filtration or the precipitation using agents that forms a specific insoluble complex with CDs. Filtration devices can be coupled to the production systems, hollow fiber and [31]. Table 1 shows the yields or concentration of CDs obtained through the action of microbial CGTase on different substrates.
Enzyme source | Substrate | Conditions | Yield (%) | Concentration (g/L) | Reference | α-cyclodextrin | 5% maltodextrin | 9 h; 50°C | 25 | 4.3 | [32] | Cassava starch | 55°C; 35 h | – | 0.32 | [33] | 5% soluble starch | 10 h; 45°C; pH 5.5 | – | 10.3 | [34] | 10% paselli SA2 | 0.1 U/mL; pH5.9; 60°C;8 h | 33 | 13.0* | [35] | β-cyclodextrin | Cassava starch | 55°C; 35 h | – | 6.33 | [33] | Starch | 26.5 | 10.6 | [36] | 5% starch | 24 h | – | 15.3 | [37] | 10% maltodextrin | 24 h | – | 21.6 | [37] | 4% starch | 72 h; 50 | – | 8.2 | [38] | 5% maltodextrin | 9 h; 50°C | 58 | 10.1 | [32] | 5% corn starch | 3 days; 60°C | – | 15.0 | [39] | 5% maltodextrin | 3 days; 60°C | – | 10.1 | [39] | 10% dextrin | 90 min; 50°C; pH 8 | – | 6.0 | [40] | 4% soluble starch | 30 s; 60°C; pH 6 | 7.9 | 1.3 | [41] | 10% starch | 24 h; 40°C; pH 8 | 45 | [42] | Soluble starch | 24 | 4.7 | [43] | 5% soluble starch | 10 h; 45°C; pH 5.5 | – | 4.1 | [34] | 10% paselli SA2 | 0.1 U/mL; pH 5.9; 60°C; 8 h | 54 | 20.0* | [35] | γ-cyclodextrin | Cassava starch | 55°C; 35 h | – | 1.02 | [33] | 5% starch | 1 h; 20% CGTase | 81.9 | 1.6 | [44] | 5% maltodextrin | 9 h; 50°C | 17 | 3.0 | [32] | 10% dextrin | 90 min; 50°C; pH 8 | – | 1.5 | [40] | Potato starch | 10 h; 50°C; pH 7 | 72.5 | [45] | 5% soluble starch | 10 h; 45°C; pH 5.5 | – | 1.8 | [34] | 15% soluble starch | 55°C; pH 12 | 47 | [46] | 10% paselli SA2 | 0.1 U/mL; pH 5.9; 60°C; 8 h | 13 | 5.0* | [35] | Mixture (α, β, and γ) | Glucans | 24 h; 40°C | 21.1 | 15.1 | [47] | 5% soluble starch | 22 h | 36.9 | [34] | 5% cassava starch | 4 h; 56°C | 55.6 | 99.5a | [48] | Tapioca starch | 4 h; 60°C | 85 | 23.0 | [49] | 15% potato starch | 24 h; 30°C; pH 5.6 | 84 | [50] | 6% sago starch | 8 h; 55°C | – | 13.7 | [51] | 8% tapioca starch | 2 h; 70°C;pH 5 | – | 12.1 | [52] | 8% tapioca starch | 3 h; 60°C | 25 | 40.0 | [49] | 50 g/L corn starch | pH 7; 45°C; 12 h; 2 U/g CGTase | 30 | – | 30% potato starch | pH 5.5–8.5; 40–55°C; 120 h;1000 U/g CGTase | 30–35 | – | [53] | 7.5% corn starch | 48 U/g CGTase; pH 6; 60°C; 24 h | 25 | – | [54] | 10% potato starch | pH 6; 50°C; 45–50 h | 40 | – | [55] | 10% potato starch | 400 U/g CGTase; pH 8; 60°C; 12 h | 34 | – | [56] | 1% soluble starch | 10 U/g; pH 5.5; 55°C; 24 h | 80 | – | [28] | 10% tapioca starch | 0.4 mmol cyclodecanone; pH 7; 25°C; 5–10 days | 91–93 | – | [57] | 1% tapioca starch | 1% toluene; pH 6; 60°C; 18 h | 15.2 | – | [58] | 12.5% wheat starch | 20 U/g CGTase; 2% butanol; pH 7.5; 40°C; 6 h | 42.5 | – | [59] | 5% soluble starch | 60°C; pH 6 | 29 | 74.0 | [60] | 5% soluble starch | 500U/g; 65°C; pH 6; 24 h | 22 | – | [61] | 5% soluble starch | 60°C; pH 6 | 30 | 75.0 | [60] |
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2.4. Alpha-glucan acting enzymes
Alpha-glucans are polysaccharides consisting of glucose units connected by α(1-4) or α(1-6) glycosidic linkages. Pullulan, a glucan produced by the fungus
Enzymes that act as hydrolyzing or debranching alpha-glucans are suitable for nondigestible oligosaccharides production. Pullulanase, dextransucrase, and starch acting enzymes can be used in the preparation of maltooligosaccharides and isomalto-oligosaccharides. Maltooligosaccharides contain α-D-glucose residues linked by α(1-4) glycosidic linkages, while isomaltooligosaccharides (IMOs) contain two to five glucose units with one or more α(1-6) linkages. While MO may exhibit immunoregulatory activity [63], the intake of IMO decreases serum cholesterol concentrations and improve bowel movement, stool output, and microbial fermentation in the colon [64]. IMOs also upregulate the Th1 response that play a triggering role in allergic diseases, such as rhinitis, asthma, and eczema [65].
Dextransucrases (EC 2.4.1.5) catalyze the synthesis of high molecular weight D-glucose polymers from sucrose to form a glucan called dextran. The synthesis of dextran occurs by successive transfer of glucosyl units to the polymer, while the presence of acceptor molecules in the reaction medium, the transfer of glucosyl units is made onto these molecules, leading to oligosaccharide synthesis. They can also transfer glucosyl units onto water molecules and simply hydrolyze sucrose [66].
Alpha-amylase (EC 3.2.1.1) also can be used to obtain maltooligosaccharides. This enzyme hydrolyses the internal α(1,4) linkages in starch in a random fashion, leading to the formation of soluble maltooligosaccharides, maltose, and glucose. A protein engineering approach of the amylase from
Pullulanase (EC 3.2.1.41), a debranching enzyme, hydrolyses the α(1-6) linkage in pullulan and branched polysaccharides, producing maltotriose. An amylopullulanase from the hyperthermophilic archaeon
Alpha-glucosidase (EC 3.2.1.20), an exo-acting hydrolase, attacks the substrates from the non-reducing end producing α-D-glucose and presents some transglycosylation activity that can be used in the production of oligosaccharides [85]. Liquefied banana slurries were used for IMO synthesis by Transglucosidase L, producing after 12 h of transglucosylation, a yield of 76.6% with a concentration of 70.74 g/L. The IMOs mixture was composed of 53 isomaltotriose, 21 isomaltotetraose, and 26% maltooligoheptaose and larger oligomers [86]. A yield of 58.1% with a concentration of 93 g/L was obtained for IMOs production from a immobilized glucosidase using as substrate a maltose solution (160 mg/mL) in a membrane reactor system [87]. Partially purified a-glucosidase from
3. Productions of NDOs through polysaccharide hydrolysis
3.1. Inulinase
Fructooligosaccharides can be produced by the controlled hydrolysis of fructans. Fructans are fructose-based polysaccharides, representing the major reserve carbohydrates in about 15% of flowering plant species [91]. According to differences in glycosidic linkages they can be classified in many types, being linear inulin the most studied and best-characterized fructan. Inulin consists of β(2-1)-linked fructose units terminating at the reducing end with a glucose residue attached through a sucrose-type linkage [92]. Inulinases can hydrolyze the β(2-1) linkages in inulin and can present endo- or exo-activity. Exo-acting inulinases (EC 3.2.1.80) produce fructose as the main end product, whereas endoinulinases (EC 3.2.1.7) act randomly and hydrolyze internal linkages of inulin to yield FOs and minor amounts of monosaccharides [93].
The highest yield (92%) for the conversion of chicory inulin (50 g/L) in to FOs was reported by the application of a dual system of
The production of FOs by a inulinase from
3.2. Xylanases
Xylan is also a heteropolysaccharide with a backbone formed by xylose homopolymer subunits linked through β(1-4) linkages. This polymer can be found in the hemicellulose fraction of lignocellulosic materials associated with lignin and cellulose. Through the hydrolysis of xylan with xylanases, xylooligosaccharides (XOs) can be produced. The intake of XOs is associated with many health benefits as improvement of bowel function, immunomodulatory, and anti-inflammatory activities, preventive effects on cancer and inhibitory effects on carcinogenesis, antimicrobial, antiallergic, and antioxidant activities [108].
The xylanase (β-1,4-d xylan xylanohydrolase, EC 3.2.1.8) is the main enzyme applied for xylan hydrolysis and XOs production, due its action on the main chain of xylan and release of oligosaccharides. Before the enzymatic hydrolysis of xylan, the hemicellulosic materials can be submitted to a pretreatment to enhance the xylan availability. Many types of pretreatments that can be performed, one approach uses NaOH or H2SO4 solutions associate with high temperatures to disrupt the hemicellulose structure. Between the substrates used for XOs production agroresidues and food by-products are highlighted due to their high contends of hemicellulose [109].
Hydrolysis of alkali pretreated corncob powder using a commercial endoxylanase produced 81 ± 1.5% of XOs in the hydrolysate equivalent to 5.8 ± 0.14 mg/mL of XOs. Reaction parameters for the production of XOs from corncob using endoxylanase from
The application of agroresidues as a source of xylan for XOs production is a strategy that has been produced excellent results. The xylan obtained by alkali extraction from cotton stalk, was hydrolyzed using a commercial xylanase preparation produced XOs in the DP range of 2–7 (X6 ≈ X5 > X2 > X3) and also minor quantities of xylose, yielding 53% (40°C; 24 h) [117]. Tobacco stalks were hydrolyzed by xylanase producing a XOs yield of 8.2%after 8 h and 11.4% after 24 h reaction period [118]. Another process yielded 7.28 and 4.52 g/L of XOs from wheat straw and rice straw xylan, respectively, after hydrolysis with a from
When sugarcane bagasse was hydrolyzed with a crude xylanase secreted by
3.3. Pectinases
Pectins are components of the cell walls of most higher plants, this heteropolysaccharide is characterized by a high content of galacturonic acid (GalA) monomers bonded together by α(1-4) linkages, showing acetylatilation or esterification with methyl groups. They are composed of homogalacturonans, xylogalacturonanes, rhamnogalacturonans, arabinans galactans, and arabinogalactans. Depending on how these polysaccharides are associated, pectin can be classified as homogalacturonan and rhamnogalacturonans I and II [136].
Studies using piglets showed that POs can modulate the grown of microbial communities in the ileum increasing, for example, the
Enzymes that act on pectins with a hydrolyzing or debranching activity have the potential to produce nondigestible oligosaccharides. The pectinolytic enzymes can be divided into: pectinesterases, pectin-methylesterases, and depolymerases being this last one more suitable for POs production. Endopolygalacturonases are depolymerases produced by various microorganisms such as bacteria, yeasts, and molds. They are also found in some plants and especially in fruits. In general, they release mono-, di-, and tri-galacturonic acid by a multiple attack mechanism single chain. Rhamnogalacturonases produce linear oligomeric compounds of alternating rhamnose and galacturonic acid (4–6 residues) with galactose residues connected to some or all the rhamnose residues. Galactanases can be divided in to endo-β-1,4-galactanases and exo-β-1,3-galactanases. The difference between these enzymes lies in their ability to hydrolyze the β(1-3), β(1-4), or β(1-6) linkages between the galactose residues [136].
Because of its high pectin content, potato, sugar beet, and apple by-products are often used as substrate for POs production. The hydrolysis of sugar beet pectin by combining endopolygalacturonase and pectinmethylesterase produced POs with a DP 1–9, with a maximum yield of trigalacturonic acid of 3.7% [140]. POs were obtained by the action of commercial enzymes on the potato rhamnogalacturonan, with a yield of 93.9 and 66.2% using Depol 670L and endo-β-1,4-galactanase, respectively. The hydrolysates yielded up to 50.6% of oligomers with DP of 13–70. Major oligosaccharides obtained with Depol 670L were DP 5 (26.3%) and DP6 (24.9%), whereas the endo-β-1,4-galactanase were DP3 (19.0%), DP5 (10.6%), and DP8 (12.6%) [141]. A high yield (93.9%) of POs was achieved using multienzymatic preparation (Depol 670 L) to hydrolyze a potato pulp by-product rich in galactan-rich rhamnogalacturonan I. Main products were oligosaccharides with DP of 2–12 (79.8–100%), whereas the oligomers with DP of 13–70 comprised smaller proportion (0.0–20.2%) [142]. A pool of pectinases was used to produce POs with degree of polymerization from 2 to 8 and six different rhamnogalacturonide structures. Total recoveries were 200 (homogalacturonides) and 67 mg/g (rhamnogalacturonides) [143]. The use of commercial pectinase preparations (Endopolygalacturonase M2, Pectinase, Viscozyme L, Pectinex Ultra SP-L, Pectinase 62 L, and Macer8 FJ) to produce POs from polygalacturonic acid. Best results were obtained with endopolygalacturonase M2 after 2 h of reaction, yielding 58, 18, and 13% of DP3 > DP2 > DP1, respectively [144].
In some cases, other food by-products were applied in the production of POs. A initial amount of 100 kg of orange peel can yield 7.5 kg of gluco-oligosaccharides, 4.5 kg of galacto-oligosaccharides, 6.3 kg of arabino-oligosaccharides, and 13 kg of oligogalacturonides [145]. Through the action commercial enzymes (EPG-M2, Viscozyme, and Pectinase) on onion skins a yield 5.6% of pectic oligosaccharides (POS) was obtained [146].
3.4. Chitosanase
Chitin is a polysaccharide formed by
A chitosanase (EC 3.2.1.132) from
4. Concluding remarks
Glycosidases are widely applied in the production of nondigestible oligosaccharides presenting easy-handed processes with high efficiency. The application of molecular biology tools to produce enzymes with new characteristics has increased the yield and productivity of NDOs. The immobilization of the enzymes and application of membrane and batch reactors are also highlighted for improvements in the production processes. Nowadays alternative substrates have been used frequently in co-products and by-products from food and agroindustry. This approach can lead to a decrease in the cost of the process and help in the correct management of these residues.
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