Microbial starch debranching enzymes: Developments and applications

Xia, Wei; Zhang, Kang; Su, Lingqia; Wu, Jang‐Yen

doi:10.1016/j.biotechadv.2021.107786

Cited by 50 publications

(21 citation statements)

References 230 publications

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“…Thus, it is critical important to develop the α-1,6-glucoside hydrolase (commonly known as starch debranching enzyme), which can effectively improve the utilization rate of raw materials and production efficiency in the process of starch hydrolysis. More importantly, this high amylose intake will not cause a sharp increase in blood glucose, and as a prebiotic, it can promote intestinal peristalsis, improve intestinal flora, and maintain intestinal health [58].…”

Section: Debranching Structure Design Of Starch Moleculesmentioning

confidence: 99%

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

Jiang²,

Kong³

et al. 2022

Syst Microbiol and Biomanuf

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As the second largest production material, starch has important value in textile, food, chemical and other fields. The shortcomings of natural starch can be solved, and its properties can be improved by modifying its structure, developing original properties, or introducing new functions, making it more suitable for certain application requirements. At present, the methods of starch modification mainly include chemical, physical, and enzymatic modification. In comparison with the two traditional modification methods (chemical and physical modification) mentioned above, enzymatic modification has the advantages of mild conditions, high substrate selectivity, and high product safety, and it is the most ideal green modification method. In this paper, we present an overview of the modified starch by enzymatic structure design. The modification process and mechanism for granule starch and gelatinized starch are summarized. Further, the difficulties encountered in starch modification by enzymatic modification were also analyzed. These analyses could pave a way for understanding and broadening the preparation and applications of modified starch, and provide theoretical references for the utilization of amylase in starch modification.

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Section: Debranching Structure Design Of Starch Moleculesmentioning

confidence: 99%

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

Jiang²,

Kong³

et al. 2022

Syst Microbiol and Biomanuf

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“…Most of the starch-degrading enzymes are classified into the glycoside hydrolase family 13 (GH13) based on the sequence-based classification . Starch-degrading enzymes are vital in starch processing and can be used for starch modification and producing glucose, maltooligosaccharides, and dextrins . In starch processing, enzymes with desirable activity and thermostability are usually preferred because a high temperature is beneficial for increasing the substrate concentration, decreasing viscosity, and avoiding bacterial contamination. , A glycogen-debranching enzyme TreX from archaea Saccharolobus solfataricus (SsGDE) is characterized as a member of the GH13 family, which can specifically act on the α-1,6 linkages in branched polysaccharides. , SsGDE is considered a potential starch-debranching enzyme that can synergistically hydrolyze the starch substrates with other starch-degrading enzymes for increasing the utilization and conversion rate of starch raw materials .…”

Section: Introductionmentioning

confidence: 99%

“…11 Starchdegrading enzymes are vital in starch processing and can be used for starch modification and producing glucose, maltooligosaccharides, and dextrins. 12 In starch processing, enzymes with desirable activity and thermostability are usually preferred because a high temperature is beneficial for increasing the substrate concentration, decreasing viscosity, and avoiding bacterial contamination. 13,14 A glycogendebranching enzyme TreX from archaea Saccharolobus solfataricus (SsGDE) is characterized as a member of the GH13 family, which can specifically act on the α-1,6 linkages in branched polysaccharides.…”

Section: Introductionmentioning

confidence: 99%

“…15,16 SsGDE is considered a potential starch-debranching enzyme that can synergistically hydrolyze the starch substrates with other starch-degrading enzymes for increasing the utilization and conversion rate of starch raw materials. 12 Via biochemical characterization, SsGDE not only exhibits high thermostability but also has a thermal activation effect through thermal treatment.…”

Section: Introductionmentioning

confidence: 99%

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Modulation of Flexible Loops in Catalytic Cavities Reveals the Thermal Activation Mechanism of a Glycogen-Debranching Enzyme

Tian

Ban

et al. 2022

J. Agric. Food Chem.

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Some thermophilic enzymes not only exhibit high thermostability at high temperatures but also have an activation effect by thermal incubation. However, the correlations between temperature-induced structural modulation and thermal activation are still unclear. In this study, we selected a thermophilic glycogen-debranching enzyme from Saccharolobus solfataricus STB09 (SsGDE), which was a promising starch-debranching enzyme with a thermal activation property at temperatures ranging from 50 to 70 °C, to explore the thermal activation mechanism. Molecular dynamics simulations were performed for SsGDE at 30, 50, or 70 °C to reveal the temperature dependence of structure modulation and catalytic function. The results revealed that four loops (loop1 313–337, loop2 399–418, loop3 481–513, and loop4 540–574) in SsGDE were reshaped, which made the catalytic cavity more open. The internal residues, including the catalytic triad Asp3631, Glu399, and Asp471, could be exposed, due to the structural modulation, to exert catalytic functions. We proposed that the thermal activation effect of SsGDE was closely associated with the temperature-induced modulation of the catalytic cavity, which paved the way for further engineering enzymes to achieve higher catalytic performance and stability.

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“…Starch hydrolysis is a standard process utilizing enzymatic saccharification, which produces a relatively clean glucose stream for further biotransformations . In contrast to chemical treatments, α-amylase-led starch hydrolysis is an effective strategy to achieve reaction specificity, improved yields, and a critical reduction in energy/water consumption during industrial processing . However, the overall cost of production and mild operating conditions required for enzymes still impede their application on an industrial scale.…”

Section: Introductionmentioning

confidence: 99%

Magnetic Halloysite Nanotube/α-Amylase Based Nanobiocatalytic Transformation of Food Processing Waste into an Active Fermentation Ingredient

Sillu

Agnihotri

Reddy

2022

ACS Sustainable Chem. Eng.

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The concept of “nanobiocatalysis” creates exciting opportunities for improving enzyme performance via immobilization onto nanomaterials. A nanobiocatalyst consisting of magnetic halloysite nanotube (MHNT)/α-amylase was evaluated to transform food processing waste into an active fermentation medium formulation for low-cost bioprocessing. A high loading of α-amylase (185.5 mg (g of support)−1) was achieved on the surface of MHNTs through polydopamine functionalization. We validated the establishment of an enzyme-support system retaining >89% catalytic activity (27332 IU (g of support)−1) with improved enzyme handling (>99.1% recovery) and reusability (>56% activity, 10 cycles). MHNTs remarkably improved the enzyme kinetics and thermodynamic characteristics along with operational and storage stabilities and mitigated the likely inhibitory effects of cellulose/metal ions as contaminants. In addition to facilitating a continuous production of reducing sugars from the extracted starch over 72 h, the nanobiocatalyst was equally effective in preparing a nutritive food waste hydrolysate as a fermentable medium substitute for batch culturing of E. coli and a single-cell protein (A. niger). The commercial relevance of waste hydrolysate was also investigated to promote calcite precipitation via Bacillus sp. induced biocementation. We evidenced that nanobiocatalyst-assisted “starch depolymerization” released more nutritional components into the hydrolysate suspension, easily accessible to growing microbial cultures.

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Microbial starch debranching enzymes: Developments and applications

Cited by 50 publications

References 230 publications

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

Engineering starch by enzymatic structure design for versatile applications in food industries: a critical review

Modulation of Flexible Loops in Catalytic Cavities Reveals the Thermal Activation Mechanism of a Glycogen-Debranching Enzyme

Magnetic Halloysite Nanotube/α-Amylase Based Nanobiocatalytic Transformation of Food Processing Waste into an Active Fermentation Ingredient

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