Maltooligosaccharide-forming amylase: Characteristics, preparation, and application

Pan, Sihui; Ding, Ning; Ren, Junyan; Gu, Zhengbiao; Li, Caiming; Yan, Hong; Cheng, Li; Holler, Tod P.; Li, Zhaofeng

doi:10.1016/j.biotechadv.2017.04.004

Cited by 74 publications

(42 citation statements)

References 84 publications

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“…In particular, α-amylase (EC 3.2.1.1) randomly cleaves the α-1,4 glycosidic linkages of starch to yield a mixture of maltodextrin, MOS and glucose. Other hydrolytic enzymes preferentially produce a particular type of MOS from starch; they are collectively known as maltooligosaccharide-forming amylases (MFAses) (Pan et al, 2017). MFAses emerge as a promising biotechnological tool given their ability to produce mainly a single type of MOS.…”

Section: Discussionmentioning

confidence: 99%

“…MFAses emerge as a promising biotechnological tool given their ability to produce mainly a single type of MOS. MFAses include maltotriose forming amylase (G3-amylase; EC 3.2.1.116), maltotetraoseforming amylase (G4-amylase; EC 3.2.1.60), maltopentaose-forming amylase (G5-amylase; EC 3.2.1.-) and maltohexaose forming amylase (G6-amylase; EC 3.2.1.98) (Pan et al, 2017). Additionally, different α-amylases may be used in combination with debranching enzymes such as pullulanase (EC 3.2.1.41) and isoamylase (EC3.2.1.68) to produce MOS from starch.…”

Section: Discussionmentioning

confidence: 99%

“…Because of this feature, they are widely used in food, pharmaceutical, cosmetic and chemical industries (Kurkov and Loftsson, 2013;Li et al, 2014;Basso et al, 2015). In turn, MOS are a novel type of functional oligosaccharides with potential applications in food industry because of their mild sweetness, relative low osmolality, high water-holding capacity and suitable viscosity, as well as their ability to inhibit crystallization and delay the staling of bread (Pan et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

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A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Castillo

Landriel

Sánchez-Costa

et al. 2018

Protein Engineering, Design and Selection

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Cyclodextrin glycosyltransferases (CGTases) are bacterial enzymes that catalyze starch conversion into cyclodextrins, which have several biotechnological applications including solubilization of hydrophobic compounds, masking of unpleasant odors and flavors in pharmaceutical preparations, and removal of cholesterol from food. Additionally, CGTases produce maltooligosaccharides, which are linear molecules with potential benefits for human health. Current research efforts are concentrated in the development of engineered enzymes with improved yield and/or particular product specificity. In this work, we analyzed the role of four residues of the CGTase from Paenibacillus barengoltzii as determinants of product specificity. Single mutations were introduced in the CGTase-encoding gene to obtain mutants A137V, A144V, L280A and M329I and the activity of recombinant proteins was evaluated. The residue at position 137 proved to be relevant for CGTase activity. Molecular dynamics studies demonstrated additionally that mutation A137V produces a perturbation in the catalytic site of the CGTase, which correlates with a 10-fold reduction in its catalytic efficiency. Moreover, this mutant showed increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose. Our results highlight the role of residue 137 as a determinant of product specificity in this CGTase and may be applied to the rational design of saccharide-producing enzymes.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Castillo

Landriel

Sánchez-Costa

et al. 2018

Protein Engineering, Design and Selection

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“…Interestingly, Y204F exhibited no G3 production, while Y204V produced G2, G3 and G5 without releasing any G1 and maltotetraose (G4) ( Wang et al, 2020 ). The abolished hydrolysis to produce G1 as the final hydrolytic product had convert this typical -amylase to a novel MFAse which was preferred in bread and high-fructose corn syrup (HFCS) industries ( Pan et al, 2017 ). However, it is worth mentioning that both Y204 and V260 were present in the -strands of central TIM-barrel which contributed to the -amylase catalytic ability.…”

Section: Survey Methodologymentioning

confidence: 99%

Native to designed: microbial α-amylases for industrial applications

Lim

Oslan

2021

PeerJ

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Background α-amylases catalyze the endo-hydrolysis of α-1,4-D-glycosidic bonds in starch into smaller moieties. While industrial processes are usually performed at harsh conditions, α-amylases from mainly the bacteria, fungi and yeasts are preferred for their stabilities (thermal, pH and oxidative) and specificities (substrate and product). Microbial α-amylases can be purified and characterized for industrial applications. While exploring novel enzymes with these properties in the nature is time-costly, the advancements in protein engineering techniques including rational design, directed evolution and others have privileged their modifications to exhibit industrially ideal traits. However, the commentary on the strategies and preferably mutated residues are lacking, hindering the design of new mutants especially for enhanced substrate specificity and oxidative stability. Thus, our review ensures wider accessibility of the previously reported experimental findings to facilitate the future engineering work. Survey methodology and objectives A traditional review approach was taken to focus on the engineering of microbial α-amylases to enhance industrially favoured characteristics. The action mechanisms of α- and β-amylases were compared to avoid any bias in the research background. This review aimed to discuss the advances in modifying microbial α-amylases via protein engineering to achieve longer half-life in high temperature, improved resistance (acidic, alkaline and oxidative) and enhanced specificities (substrate and product). Captivating results were discussed in depth, including the extended half-life at 100 °C, pH 3.5 and 10, 1.8 M hydrogen peroxide as well as enhanced substrate (65.3%) and product (42.4%) specificities. These shed light to the future microbial α-amylase engineering in achieving paramount biochemical traits ameliorations to apt in the industries. Conclusions Microbial α-amylases can be tailored for specific industrial applications through protein engineering (rational design and directed evolution). While the critical mutation points are dependent on respective enzymes, formation of disulfide bridge between cysteine residues after mutations is crucial for elevated thermostability. Amino acids conversion to basic residues was reported for enhanced acidic resistance while hydrophobic interaction resulted from mutated hydrophobic residues in carbohydrate-binding module or surface-binding sites is pivotal for improved substrate specificity. Substitution of oxidation-prone methionine residues with non-polar residues increases the enzyme oxidative stability. Hence, this review provides conceptual advances for the future microbial α-amylases designs to exhibit industrially significant characteristics. However, more attention is needed to enhance substrate specificity and oxidative stability since they are least reported.

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“…Structurally, they consist of 3-10 α-D-glucopyranosyl units linked by α-1,4 glycosidic bonds. Given their high water solubility, mild sweetness, and suitable viscosity, maltooligosaccharides are considered palatable and superior nutrient foods for the aged and infants (Pan et al, 2017). In particular, maltopentaose (G5), which contains five glucosyl units, is essential in medical and pharmaceutical fields for its use as a dietary nutrient for patients having renal failure or calorie deprivation and as a diagnostic reagent for the detection of α-amylase in serum and urine (Kandra, 2003;Wang et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine Bacterium Saccharophagus degradans 2-40T

et al. 2021

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Marine extremophiles produce cold-adapted and/or salt-tolerant enzymes to survive in harsh conditions. These enzymes are naturally evolved with unique structural features that confer a high level of flexibility, solubility and substrate-binding ability compared to mesophilic and thermostable homologs. Here, we identified and characterized an amylase, SdG5A, from the marine bacterium Saccharophagus degradans 2-40T. We expressed the protein in Bacillus subtilis and found that the purified SdG5A enabled highly specific production of maltopentaose, an important health-promoting food and nutrition component. Notably, SdG5A exhibited outstanding cold adaptation and salt tolerance, retaining approximately 30 and 70% of its maximum activity at 4°C and in 3 M NaCl, respectively. It converted 68 and 83% of starch into maltooligosaccharides at 4 and 25°C, respectively, within 24 h, with 79% of the yield being the maltopentaose. By analyzing the structure of SdG5A, we found that the C-terminal carbohydrate-binding module (CBM) coupled with an extended linker, displayed a relatively high negative charge density and superior conformational flexibility compared to the whole protein and the catalytic domain. Consistent with our bioinformatics analysis, truncation of the linker-CBM region resulted in a significant loss in activities at low temperature and high salt concentration. This highlights the linker-CBM acting as the critical component for the protein to carry out its activity in biologically unfavorable condition. Together, our study indicated that these unique properties of SdG5A have great potential for both basic research and industrial applications in food, biology, and medical and pharmaceutical fields.

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Maltooligosaccharide-forming amylase: Characteristics, preparation, and application

Cited by 74 publications

References 84 publications

A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Native to designed: microbial α-amylases for industrial applications

Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine Bacterium Saccharophagus degradans 2-40T

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