Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications

Nakapong, Santhana; Tumhom, Suthipapun; Kaulpiboon, Jarunee; Pongsawasdi, Piamsook

doi:10.1007/s11274-021-03220-1

Cited by 8 publications

(9 citation statements)

References 151 publications

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“…Despite the fact that a large number of AMs have been effectively produced in E. coli hosts, some food and pharmaceutical applications may demand safer manufacturing. Thus, some AMs were studied to express in GRAS (generally recognized as safe) hosts such as Bacillus subtilis and Saccharomyces cerevisiae to be served in the applications in those fields [10]. TaAM, which had been successfully expressed in B. subtilis, had its safety assessed in mice, demonstrating that it was sufficiently safe for food applications [22].…”

Section: Sources and Biochemical Properties Of Amylomaltasementioning

confidence: 99%

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Production of Large-Ring Cyclodextrins by Amylomaltases

et al. 2022

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Amylomaltase is a well-known glucan transferase that can produce large ring cyclodextrins (LR-CDs) or so-called cycloamyloses via cyclization reaction. Amylomaltases have been found in several microorganisms and their optimum temperatures are generally around 60–70 °C for thermostable amylomaltases and 30–45 °C for the enzymes from mesophilic bacteria and plants. The optimum pHs for mesophilic amylomaltases are around pH 6.0–7.0, while the thermostable amylomaltases are generally active at more acidic conditions. Size of LR-CDs depends on the source of amylomaltases and the reaction conditions including pH, temperature, incubation time, and substrate. For example, in the case of amylomaltase from Corynebacterium glutamicum, LR-CD productions at alkaline pH or at a long incubation time favored products with a low degree of polymerization. In this review, we explore the synthesis of LR-CDs by amylomaltases, structural information of amylomaltases, as well as current applications of LR-CDs and amylomaltases.

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Section: Sources and Biochemical Properties Of Amylomaltasementioning

confidence: 99%

“…A few articles reviewing 4αGTases have been published recently. Nakapong et al, 2022 focused on heterologous expression of 4αGTases including CGTase and amylomaltase for overproduction and beneficial properties for industrial applications [10]. Leoni and co-workers emphasized thermostability of amylomaltases from the extremophiles [11].…”

Section: Introductionmentioning

confidence: 99%

Production of Large-Ring Cyclodextrins by Amylomaltases

et al. 2022

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“…However, CGTase production from wild-type organisms results in lower yields that [39,40] can be enhanced using various strategies, such as culture medium optimization through a stepwise approach or statistical media optimization approach [36,38,[41][42][43][44][45][46][47][48][49]. Moreover, enzyme overproduction can be achieved through heterologous enzyme expression [7,50]. Various reports have also demonstrated CGTase expression on the cell surface of various hosts.…”

Section: Production and Properties Of Cgtasementioning

confidence: 99%

“…Heterologous production strategies can improve enzymatic expression through protein engineering, and codon optimization of genes based on the host organism [52]. Other recombinant hosts are also used for CGTase production, such as Bacillus subtilis and Pichia pastoris, because they offer extracellular secretion together with higher yields [7,50]. Among various heterologous expression hosts, E. coli is the most popular host for CGTase expression because of its easy and rapid cultivation, low cost of enzyme production, high protein yields, and easy system for foreign gene expression [50,53].…”

Section: Production and Properties Of Cgtasementioning

confidence: 99%

“…Other recombinant hosts are also used for CGTase production, such as Bacillus subtilis and Pichia pastoris, because they offer extracellular secretion together with higher yields [7,50]. Among various heterologous expression hosts, E. coli is the most popular host for CGTase expression because of its easy and rapid cultivation, low cost of enzyme production, high protein yields, and easy system for foreign gene expression [50,53]. Heterologous expression of CGTase from Paenibacillus sp.…”

Section: Production and Properties Of Cgtasementioning

confidence: 99%

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Microbial Cyclodextrin Glycosyltransferases: Sources, Production, and Application in Cyclodextrin Synthesis

Gupta¹,

Tyagi²,

Pathak³

et al. 2022

Catal Res

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Cyclodextrin glycosyltransferase (CGTase) is a multifunctional enzyme that hydrolyzes the α-glycosidic bond between two sugar molecules and synthesizes cyclodextrins (CDs) and other transglycosylation products. It is a ubiquitously present extracellular enzyme that offers the CGTase-producing organism the sole right onto starch substrates over other microbes. The present review provides a brief account of diversity among CGTase-producing microbes, CGTase production in different heterologous hosts (wherein extracellular secretion is highly desired), and different physicochemical properties of CGTases. Overall, 52 crystal structures that highlight the five domain tertiary structure of CGTases have been discovered so far. On the basis of these structures, the catalytic mechanism of CGTase reactions has been discussed, and three catalytic residues, namely Glu257, Asp229, and Asp328, have been identified at the active site in all CGTases. Moreover, the active site is constituted by at least nine sugar-binding sites, denoted as -7 to +2. Furthermore, a sequence alignment of selected CGTases highlighted the conserved regions and the sequential differences among α-CGTases, β-CGTases, and γ-CGTases. Various biotechnological applications of CGTases and CGTase immobilization on a variety of support matrices are briefly discussed. This review also encompasses a detailed account of CDs, their enzymatic production, extraction, and applications in different industrial sectors.

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