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HPLC results for glucose, isomaltose and isomaltotriose (a); and for the final products of dextranase (b).
Source publication
A novel dextranase was purified from Penicillium cyclopium CICC-4022 by ammonium sulfate fractional precipitation and gel filtration chromatography. The effects of temperature, pH and some metal ions and chemicals on dextranase activity were investigated. Subsequently, the dextranase was used to produce dextran with specific molecular mass. Weight-...
Contexts in source publication
Context 1
... our dextranase showed high specificity toward dextrans that contain mostly α-1,6 glucosidic bond and it was inactive with the α-1,4, β-1,2, β-1,4 glucosidic bonds of the substrate. (Figure 5a). The peaks of our final products of dextranase were consistent with the peaks of glucose, isomaltose and isomaltotriose (Figure 5a). ...
Context 2
... 5a). The peaks of our final products of dextranase were consistent with the peaks of glucose, isomaltose and isomaltotriose (Figure 5a). It is known that the final products of endodextranase were mainly isomaltose, isomaltotriose and a small amount of glucose [2]. ...
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... our dextranase showed high specificity toward dextrans that contain mostly α-1,6 glucosidic bond and it was inactive with the α-1,4, β-1,2, β-1,4 glucosidic bonds of the substrate. HPLC results show that the peaks of glucose, isomaltose and isomaltotriose appeared at 6.6, 10.4 and 17.4 min, respectively (Figure 5a). The peaks of our final products of dextranase were consistent with the peaks of glucose, isomaltose and isomaltotriose (Figure 5a). ...
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... results show that the peaks of glucose, isomaltose and isomaltotriose appeared at 6.6, 10.4 and 17.4 min, respectively (Figure 5a). The peaks of our final products of dextranase were consistent with the peaks of glucose, isomaltose and isomaltotriose (Figure 5a). It is known that the final products of endodextranase were mainly isomaltose, isomaltotriose and a small amount of glucose [2]. ...
Citations
... is an enzyme commonly applied in food [1], sugar making [2], medicine [3], and biotechnology fields [4]. It exhibits specific hydrolytic activity toward α-1,6 glycosidic bonds [5]. Based on their structural characteristics, dextranases are classified into GH49 and GH66 families. ...
Dextranase (EC 3.2.1.11) is primarily applied in food, sugar, and pharmaceutical industries. This study focuses on using a cold shock Escherichia coli expression system to express marine dextranase SP5-Badex; enzyme activity increased about 2.2-fold compared to previous expression. This enzyme was employed to produce sweet potato porous starch, with special emphasis on the pore size of the starch. The water and oil adsorption rates of the porous starch increased by 1.43 and 1.51 times, respectively. Extensive Fourier transform infrared spectroscopy and X-ray diffraction revealed that the crystal structure of the sweet potato starch was unaltered by enzymatic hydrolysis. The adsorption capacities of the porous starch for curcumin and proanthocyanidins were 9.59 and 12.29 mg/g, respectively. Notably, the stability of proanthocyanidins was significantly enhanced through their encapsulation in porous starch. After 2.5 h of ultraviolet irradiation, the free radical scavenging rate of the encapsulated proanthocyanidins remained at 95.10%. Additionally, after 30 days of sunlight exposure, the free radical scavenging rate of the encapsulated proanthocyanidins (84.42%) was significantly higher than that (24.34%) observed in the control group. These research findings provide substantial experimental evidence for preparing sweet potato porous starch using marine dextranase.
... Our results are in general agreement with that observed by Hayacibara et al. (2004), which show that a mutanase from Trichoderma harzianum and a dextranase from Penicillium aculeatum effectively reduced the total amount of polysaccharides produced by Streptococci bacteria. Furthermore, our findings are in line with previous reports on the efficacy of mutanases and dextranases in preventing the formation of oral streptococcal biofilms (Hawkey et al. 1984;Yano et al. 2006;Suzuki et al. 2015;Buddana et al. 2019;Huang et al. 2019). Regarding enzymatic treatment on pre-formed biofilms, our results clearly demonstrate a substantial decrease in total biomass and extracellular polysaccharides amount of pre-formed S. mutans biofilms. ...
... The optimal pH and temperature conditions identified for PmGH87 activity were similar to those determined for mutanases rAglST1 and rAglST2 as described by Cherdvorapong et al. (2020) and Agl-FH1 e Agl-FH2 as reported by Suyotha et al. (2014). The optimum pH and T of CoGH66 dextranase were at the same range of other dextranases (Hoster et al. 2001;Finnegan et al. 2004;Park et al. 2012;Wang et al. 2016;Huang et al. 2019). Furthermore, the optimal conditions for PmGH87 and CoGH66 thermal stability determined by Thermofluor are broadly consistent with their pH and temperature profiles (Supplementary Figures S2 and S3). ...
Dental biofilms represent a serious oral health problem playing a key role in the development of caries and other oral diseases. In the present work, we cloned and expressed in E. coli two glucanases, Prevotella melaninogenica mutanase (PmGH87) and Capnocytophaga ochracea dextranase (CoGH66), and characterized them biochemically and biophysically. Their three-dimensional structures were elucidated and discussed. Furthermore, we tested the capacity of the enzymes to hydrolyze mutan and dextran to prevent formation of Streptococcus mutans biofilms, as well as to degrade pre- formed biofilms in low and abundant sugar conditions. The percentage of residual biofilm was calculated for each treatment group in relation to the control, as well as the degree of synergism. Our results suggest that both PmGH87 and CoGH66 are capable of inhibiting biofilm formation grown under limited or abundant sucrose conditions. Degradation of pre-formed biofilms experiments reveal a time-dependent effect for the treatment with each enzyme alone. In addition, a synergistic and dose-dependent effects of the combined enzymatic treatment with the enzymes were observed. For instance, the highest biomass degradation was 95.5% after 30 min treatment for the biofilm grown in low sucrose concentration, and 93.8% after 2 h treatment for the biofilm grown in sugar abundant condition. Strong synergistic effects were observed, with calculated degree of synergism of 5.54 and 3.18, respectively and their structural basis was discussed. Jointly, these data can pave the ground for the development of biomedical applications of the enzymes for controlling growth and promoting degradation of established oral biofilms.
... However, the fermentation process for bacterial dextranases is usually shorter and results in fewer harmful byproducts [11]. the level of acidity, the content of solids, temperature, contact time, agitation, dextran con- 48 centration, as well as the source, activity, and dosage of the enzyme [12,13]. This research 49 aimed to explore the synthesis of dextranase through marine bacteria. ...
... After 48 h of fermentation at 25 • C and 180 rpm, dextranase activity was measured using an adapted method [12]. The strain with the highest dextranase activity was selected for further study. ...
... The dextranase enzyme solution of 50 µL was combined with 75 µL of 3% dextran T20 in a 75 mM pH 6.0 Tris-HCl buffer, and this mixture was incubated at 40 • C for 30 min. Subsequently, the concentration of reduced sugar in the mixture was determined using the DNS method [12]. The enzyme activity was defined as the quantity of the enzyme needed to catalyze the release of 1 µmol of maltose per minute under the above-mentioned reaction conditions. ...
Dextranase, also known as glucanase, is a hydrolase enzyme that cleaves α-1,6 glycosidic bonds. In this study, a dextranase-producing strain was isolated from water samples of the Qingdao Sea and identified as Microbacterium sp. This strain was further evaluated for growth conditions, enzyme-producing conditions, enzymatic properties, and hydrolysates. Yeast extract and sodium chloride were found to be the most suitable carbon and nitrogen sources for strain growth, while sucrose and ammonium sodium were found to be suitable carbon and nitrogen sources for fermentation. The optimal pH was 7.5, with a culture temperature of 40 °C and a culture time of 48 h. Dextranase produced by strain XD05 showed good thermal stability at 40 °C by retaining more than 70% relative enzyme activity. The pH stability of the enzyme was better under a weak alkaline condition (pH 6.0–8.0). The addition of NH4+ increased dextranase activity, while Co2+ and Mn2+ had slight inhibitory effects on dextranase activity. In addition, high-performance liquid chromatography showed that dextran is mainly hydrolyzed to maltoheptanose, maltohexanose, maltopentose, and maltootriose. Moreover, it can form corn porous starch. Dextranase can be used in various fields, such as food, medicine, chemical industry, cosmetics, and agriculture.
... Nowadays, a variety of dextranase-producing microbes, comprising bacteria, filamentous fungi, and yeast strains as shown in Fig. 1. (Abdel-Naby et al. 1999;Bhatia et al. 2010;Erhardt and Jördening 2007), have been reported. Bacteria and fungi are typically considered to be the most significant and primary sources of dextranase (Abdelwahed et al. 2014;Deng et al. 2020;Huang et al. 2019;Ning et al. 2021). Dextranases are reportedly synthesized with a high yield by the bacterial genera Bacillus (Abdel-Naby et al. 1999;Khalikova et al. 2003;Zohra et al. 2015), Shewanella (Liu et al. 2020), Thermoanaerobacter (Suzuki et al. 2015), Cytophaga (Janson 1975), Paenibacillus (Hild et al. 2007;Janson 1975;Suzuki et al. 2015), Arthrobacter (Lee et al. 2010), and Streptococcus (Pulkownik and Walker 1977). ...
... Dextranases are reportedly synthesized with a high yield by the bacterial genera Bacillus (Abdel-Naby et al. 1999;Khalikova et al. 2003;Zohra et al. 2015), Shewanella (Liu et al. 2020), Thermoanaerobacter (Suzuki et al. 2015), Cytophaga (Janson 1975), Paenibacillus (Hild et al. 2007;Janson 1975;Suzuki et al. 2015), Arthrobacter (Lee et al. 2010), and Streptococcus (Pulkownik and Walker 1977). The fungi Paecilomyces lilacinus (Bhatia et al. 2010), Penicillium (Huang et al. 2019;Mahmoud et al. 2014), Talaromyces (Zhang et al. 2017), Aspergillus (Netsopa et al. 2019), Hypocrea (Wu et al. 2011), Pochonia (Virgen-Ortíz et al. 2015. ...
... NK458 (Purushe et al. 2012) and Chaetomium gracile (Zhao et al. 2021), which itself provide rapid responsiveness enzyme activity varying from pH 5.0 to 10.0 (> 50% activity), the enzymatic activity might only be sustained at a reasonably high level in an environment that was either neutral or slightly alkaline. There is evidence that some metal ions, such as Fe2 + and Li+, may stimulate the action of dextranase (Huang et al. 2019). In addition, the presence of Co2+, Mn2+, and Ca2 + caused an acceleration in the activity of dextranase extracted from A. allahabadii X26 (Netsopa et rate of reaction. ...
Dextranase is a type of hydrolase that is responsible for catalyzing the breakdown of high-molecular-weight dextran into low-molecular-weight polysaccharides. This process is called dextranolysis. A select group of bacteria and fungi, including yeasts and likely certain complex eukaryotes, produce dextranase enzymes as extracellular enzymes that are released into the environment. These enzymes join dextran's α-1,6 glycosidic bonds to make glucose, exodextranases, or isomalto-oligosaccharides (endodextranases). Dextranase is an enzyme that has a wide variety of applications, some of which include the sugar business, the production of human plasma replacements, the treatment of dental plaque and its protection, and the creation of human plasma replacements. Because of this, the quantity of studies carried out on worldwide has steadily increased over the course of the past couple of decades. The major focus of this study is on the most current advancements in the production, administration, and properties of microbial dextranases. This will be done throughout the entirety of the review.
... There are abundant sources of dextranase, which can be produced by higher organisms and microorganisms. Since the first report of Cellvibrio fulva dextranase in 1940 (Hultin et al., 1967), more than 100 patents have been issued on dextran-hydrolyzing enzymes found in a number of microbial groups (Abdelwahed et al., 2014;Deng et al., 2020;Dong et al., 2021;Huang et al., 2019;Khalikova et al., 2003;Lee et al., 2010;H. Liu et al., 2019;N. ...
Dextranase is an important industrial enzyme for the preparation of isomalto‐oligosaccharides. According to the crystal structures of 20 dextranases of four classes, we summarized the structural characteristics of enzymes and the binding modes of enzymes and ligands in this paper. Based on the characteristics of the products, we analyzed the characteristics of the binding domain and functions of dextranase by means of molecular simulation and molecular docking. The relationship between the product specificity of dextranase, its catalytic pocket shape, and its catalytic mode was briefly summarized. The catalytic mechanism of dextranase was systematically discussed, which provided the basis and reference for the rational transformation of dextranase. There are highly flexible amino acid residues in the vicinity of the catalytic domain of dextranase, which affect substrate binding and product discharge. Generally, whether endo‐ or exo‐type dextranase, their −1 and −2 sites in catalytic domain are conserved and play a key role in substrate recognition. The exo‐dextranases recognize the nonreducing end and the endo‐dextranases recognize α‐1,6 glycosidic bond inside dextran chain randomly through the shape of the pocket.
... The developed color was measured using a spectrophotometer at 540 nm (13). One unit (1U) of dextranase activity was defined as the amount of enzyme that degrades dextran to produce 1 μmol of glucose equivalent per min at 37°C with pH 7 (14,15). A calibration curve was constructed using standard glucose solutions and a series of dilutions from 0.05 to 1mg/ml (14). ...
Background and Objectives: Dental caries is a breakdown of the teeth enamel due to harmful bacteria, lack of oral hygiene, and sugar consumption. The acid-producing bacterium Streptococcus mutans is the leading cause of dental caries. Dextranase is an enzyme that can degrade dextran to low molecular weight fractions, which have many therapeutic and industrial applications. The purpose of the present study was to isolate a novel dextranase-producing bacteria from a source (molasses). The cell-free extracts containing dextranases were tested as antibiofilm agents.
Materials and Methods: Dextranase-producing bacteria were identified using phenotypic and genotypic methods such as 16S rRNA gene sequencing and enzymatic characterization.
Results: The highest six dextranase-producing bacterial isolates were Bacillus species. The best conditions for dextranase productivity were obtained after 72 hours of culture time at pH 7. The addition of glucose to the medium enhanced the production of the enzymes. The cell-free extract of the six most active isolates showed remarkable activity against biofilm formation by Streptococcus mutans ATCC 25175. The highest inhibition activities reached 60% and 80% for Bacillus velezensis and Pseudomonas stutzeri, respectively.
Conclusion: Therefore, our study added to the current dextranase-producing bacteria with potential as a source of dextranases.
... Dextranases are classified into glycoside hydrolase (GH) 49, 66, 27 and 31 families based on protein structures and sequence similarity (Okazawa et al., 2015;Ren et al., 2019;Tsutsumi et al., 2019). Fungal dextranases often had high activity (generally more than 100 U/mg), but they possessed poor thermal stability and were also unstable under alkaline conditions (Huang et al., 2019). Their optimistic temperature was frequently higher than 50°C, and the optimistic pH was lower than 7 (Khalikova et al., 2005;Zhao et al., 2020;Pittrof et al., 2021). ...
... The K m of CeDex for dextran T70 was 0.0991 mM, less than those of dextranases from Arthrobacter oxydans (4.73 mM), Aspergillus allahabadii X26 (14.29 mM), Penicillium cyclopium CICC-4022 (2.61 mM) and Streptomyces sp. NK458 (94.30 mM; Huang et al., 2019), demonstrating the stronger affinity of CeDex for dextran. The K cat and K cat /K m values of CeDex for dextran T20 were the highest, indicating that CeDex had higher catalytic efficiency for dextran T20 than T10 and T70. ...
The cold-adapted and/or salt-tolerant enzymes from marine microorganisms were confirmed to be meritorious tools to enhance the efficiency of biocatalysis in industrial biotechnology. We purified and characterized a dextranase CeDex from the marine bacterium Cellulosimicrobium sp. THN1. CeDex acted in alkaline pHs (7.5–8.5) and a broad temperature range (10–50°C) with sufficient pH stability and thermostability. Remarkably, CeDex retained approximately 40% of its maximal activities at 4°C and increased its activity to 150% in 4 M NaCl, displaying prominently cold adaptation and salt tolerance. Moreover, CeDex was greatly stimulated by Mg2+, Na+, Ba2+, Ca2+ and Sr2+, and sugarcane juice always contains K+, Ca2+, Mg2+ and Na+, so CeDex will be suitable for removing dextran in the sugar industry. The main hydrolysate of CeDex was isomaltotriose, accompanied by isomaltotetraose, long-chain IOMs, and a small amount of isomaltose. The amino acid sequence of CeDex was identified from the THN1 genomic sequence by Nano LC–MS/MS and classified into the GH49 family. Notably, CeDex could prevent the formation of Streptococcus mutans biofilm and disassemble existing biofilms at 10 U/ml concentration and would have great potential to defeat biofilm-related dental caries.
... The bacterial genera, Bacillus [15][16][17][18], Shewanella [19], Thermoanaerobacter [20], Arthrobacter [21], Cytophaga [22], Paenibacillus [23][24][25] and Streptococcus [26] have been reported to produce dextranases in good yield. Among fungal species, Paecilomyces lilacinus [27] and the species of Penicillium [28,29], Hypocrea [30], Pochonia [31], Chaetomium [32], Talaromyces [3], and Aspergillus [33] are reportedly promising producers of dextranases. The microbial sources of dextranases from marine environment have also been described, from bacteria [34][35][36][37] and from fungi [38]. ...
... In the Table 1, a list of the purification strategies used for purifying these dextranases is depicted. Table 1 represents dextranases from microorganisms that use Dextran T500 as a nutrient medium which hydrolyze α-1.6 bonds [29]. For the purification of dextranases, Ren et al. [74] used the following methods in comparison: ultrafiltration, ethanol precipitation, ammonium sulfate precipitation, thin layer and ion exchange chromatography [34]. ...
Dextran, a renewable hydrophilic polysaccharide, is nontoxic, highly stable but intrinsically biodegradable. The α-1, 6 glycosidic bonds in dextran are attacked by dextranase (E.C. 3.2.1.11) which is an inducible enzyme. Dextranase finds many applications such as, in sugar industry, in the production of human plasma substitutes, and for the treatment and prevention of dental plaque. Currently, dextranases are obtained from terrestrial fungi which have longer duration for production but not very tolerant to environmental conditions and have safety concerns. Marine bacteria have been proposed as an alternative source of these enzymes and can provide prospects to overcome these issues. Indeed, marine bacterial dextranases are reportedly more effective and suitable for dental caries prevention and treatment. Here, we focused on properties of dextran, properties of dextran-hydrolyzing enzymes, particularly from marine sources and the biochemical features of these enzymes. Lastly the potential use of these marine bacterial dextranase to remove dental plaque has been discussed. The review covers dextranase-producing bacteria isolated from shrimp, fish, algae, sea slit, and sea water, as well as from macro-and micro fungi and other microorganisms. It is common knowledge that dextranase is used in the sugar industry; produced as a result of hydrolysis by dextranase and have prebiotic properties which influence the consistency and texture of food products. In medicine, dextranases are used to make blood substitutes. In addition, dextranase is used to produce low molecular weight dextran and cytotoxic dextran. Furthermore, dextranase is used to enhance antibiotic activity in endocarditis. It has been established that dextranase from marine bacteria is the most preferable for removing plaque, as it has a high enzymatic activity. This study lays the groundwork for the future design and development of different oral care products, based on enzymes derived from marine bacteria.
... μmol/(mg·min). Most dextranases had Km values between 1-10 mg/mL for the dextran substrate, and the smaller the Km value, the higher affinity for the substrate [9,20,21]. The results indicated that the enzyme has a fine affinity for the substrate dextran T500. ...
... µmol/(mg·min). Most dextranases had Km values between 1-10 mg/mL for the dextran substrate, and the smaller the Km value, the higher affinity for the substrate [9,20,21]. The results indicated that the enzyme has a fine affinity for the substrate dextran T500. ...
... Component Analysis of PsDex1711 Hydrolysate 4.9.1. DPPH Radical Scavenging Rate PsDex1711 and dextran T70 were mixed at a ratio of 1:3, reacted at 30 • C for 4 h to obtain the hydrolysate, lyophilized for 24 h, and configured into hydrolysates of different concentrations (20,40,60,80, and 100 mg/mL). Then, 200 µL of PsDex1711 hydrolysates of different concentrations was mixed with 0.1 mM DPPH (absolute ethanol configuration). ...
Intestinal diseases are mainly caused by a decrease in the relative abundance of probiotics and an increase in the number of pathogenic bacteria due to dysbiosis of the intestinal flora. High degree polymerization isomaltooligosaccharide (IMO) can promote probiotic metabolism and proliferation. In this study, the dextranase (PsDex1711) gene of marine bacterial Pseudarthrobacter sp. RN22 was cloned and expressed in Escherichia coli BL21 (DE3). The optimal pH and temperature of the dextranase were 6.0 and 30 °C, respectively, showing the highest stability at 20 °C. The dextran T70 could be hydrolyzed to produce IMO3, IMO4, IMO5, and IMO6 with a high degree of polymerization. The hydrolysate of 1 mg/mL could significantly promote the growth of Lactobacillus and Bifidobacterium after 12 h culture and the formation of biofilms by 58.2%. The hydrolysates could promote the proliferation of probiotics. Furthermore, the IC50 of scavenging rate of DPPH, hydroxyl radical, and superoxide anion was less than 20 mg/mL. This study provides a crucial theoretical basis for the application of dextranase such as pharmaceutical and food industries.
... NK458 (Purushe et al., 2012) and Chaetomium gracile (Zhao et al., 2021), which displayed high enzyme activity ranging from pH 5.0 to 10.0 (>50% activity). Certain metal ions exhibited to promote dextranase activity, for example, Fe 2+ and Li + (Huang et al., 2019). Moreover, contrary to the results of our study, the existence of Co 2+ , Mn 2+ , Ca 2+ accelerated the activity of dextranase from A. allahabadii X26 (Netsopa et al., 2019). ...
Dextran has aroused increasingly more attention as the primary pollutant in sucrose production and storage. Although enzymatic hydrolysis is more efficient and environmentally friendly than physical methods, the utilization of dextranase in the sugar industry is restricted by the mismatch of reaction conditions and heterogeneity of hydrolysis products. In this research, a dextranase from Arthrobacter oxydans G6-4B was purified and characterized. Through anion exchange chromatography, dextranase was successfully purified up to 32.25-fold with a specific activity of 288.62 U/mg protein and a Mw of 71.12 kDa. The optimum reaction conditions were 55°C and pH 7.5, and it remained relatively stable in the range of pH 7.0–9.0 and below 60°C, while significantly inhibited by metal ions, such as Ni⁺, Cu²⁺, Zn²⁺, Fe³⁺, and Co²⁺. Noteworthily, a distinction of previous studies was that the hydrolysates of dextran were basically isomalto-triose (more than 73%) without glucose, and the type of hydrolysates tended to be relatively stable in 30 min; dextranase activity showed a great influence on hydrolysate. In conclusion, given the superior thermal stability and simplicity of hydrolysates, the dextranase in this study presented great potential in the sugar industry to remove dextran and obtain isomalto-triose.
