Maltooligosaccharides production catalysed by cyclodextrin glycosyltransferase from Bacillus circulans DF 9R in batch and continuous operation

Gastón, Jorgelina A. Rodríguez; Costa, Hernán; Rossi, Ana Lía; Krymkiewicz, Norberto; Ferrarotti, Susana Alicia

doi:10.1016/j.procbio.2012.08.008

Cited by 15 publications

(4 citation statements)

References 18 publications

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“…CGTases can use a variety of carbohydrates and other compounds as acceptors in intermolecular transglucosylation reactions; however, the conversion rates of acceptors are quite different. For example, the glucose conversion rate observed using Bacillus macerans CGTase and the maltose conversion rate observed using Bacillus circulans DF 9R CGTase were 97% and 60%, respectively. , The conversion rate of l -AA observed using Paenibacillus macerans CGTase was only 9% . The relatively poor l -AA conversion rate may be attributed to the fact that the natural acceptors of CGTase are carbohydrate molecules.…”

Section: Introductionmentioning

confidence: 94%

Enhanced 2-O-α-d-Glucopyranosyl-l-ascorbic Acid Synthesis through Iterative Saturation Mutagenesis of Acceptor Subsite Residues in Bacillus stearothermophilus NO2 Cyclodextrin Glycosyltransferase

Tao

Wang

et al. 2018

J. Agric. Food Chem.

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Low synthesis yields of the l-ascorbic acid (l-AA) derivative 2- O-α-d-glucopyranosyl-l-ascorbic acid (AA-2G) limit its application in the food industry. In this work, the AA-2G synthesis yield of Bacillus stearothermophilus NO2 cyclodextrin glycosyltransferase (CGTase) was improved. Nine residues within 10 Å of the catalytic residue Glu displaying ≤30% conservation and located in the acceptor subsite were selected for iterative saturation mutagenesis. The best mutant, K228R/M230L, produced a higher AA-2G yield with maltodextrin as the glucosyl donor than that produced by its parent wild-type. The l-AA K values of the mutant K228R/M230L decreased by 35%, whereas the k/ K increased by 2.69-fold. Kinetic analysis indicated that K228R/M230L displayed enhanced l-AA specificity. These results demonstrate that acceptor subsite residues play an important role in acceptor substrate specificity. Mutant K228R/M230L afforded the highest AA-2G concentration (211 g L, 624 mM) reported to date after optimization of the reaction conditions.

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Section: Introductionmentioning

confidence: 94%

Enhanced 2-O-α-d-Glucopyranosyl-l-ascorbic Acid Synthesis through Iterative Saturation Mutagenesis of Acceptor Subsite Residues in Bacillus stearothermophilus NO2 Cyclodextrin Glycosyltransferase

Tao

Wang

et al. 2018

J. Agric. Food Chem.

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“…The reactor operation in a continuous regime can provide a 12% higher yield than the batch process. Adding glucose or maltose to the reaction mixture can further increase MOS production [ 123 ].…”

Section: Overview Of Different Ways Of Producing Maltooligosaccharidesmentioning

confidence: 99%

Maltooligosaccharides: Properties, Production and Applications

et al. 2023

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Maltooligosaccharides (MOS) are homooligosaccharides that consist of 3–10 glucose molecules linked by α-1,4 glycosidic bonds. As they have physiological functions, they are commonly used as ingredients in nutritional products and functional foods. Many researchers have investigated the potential applications of MOS and their derivatives in the pharmaceutical industry. In this review, we summarized the properties and methods of fabricating MOS and their derivatives, including sulfated and non-sulfated alkylMOS. For preparing MOS, different enzymatic strategies have been proposed by various researchers, using α-amylases, maltooligosaccharide-forming amylases, or glycosyltransferases as effective biocatalysts. Many researchers have focused on using immobilized biocatalysts and downstream processes for MOS production. This review also provides an overview of the current challenges and future trends of MOS production.

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“…Cassava starch (50 mg/ ml) was incubated in sodium phosphate buffer pH 6.4 with 1.2 μg of enzyme per gram of substrate during 4 h at 56°C and 100 rpm. For MOS production, the above reaction mixture was supplemented with 50 mg/ml glucose and incubation lasted for 24 h at 56°C and 100 rpm (Rodríguez Gastón et al, 2012). The enzyme was inactivated by treatment at 100°C for 5 min.…”

Section: Production Of CD and Mos From Starchmentioning

confidence: 99%

“…As other α-glucanotransferases, the enzyme also catalyzes α-1,4 intermolecular transglycosylation reactions by opening of CD and subsequent transference to non-reducing ends of acceptors (coupling) or by transferring one chain of linear oligosaccharides to another chain of linear oligosaccharides (disproportionation) (Van Der Maarel and Leemhuis, 2013). The latter reactions lead to the biosynthesis of α-1,4 linear dextrins (maltooligosaccharides, MOS) with different degrees of polymerization according to the nature of the acceptor employed (Rodríguez Gastón et al, 2012). Additionally, CGTases also exhibit weak amylolytic activity (van der Veen et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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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Maltooligosaccharides production catalysed by cyclodextrin glycosyltransferase from Bacillus circulans DF 9R in batch and continuous operation

Cited by 15 publications

References 18 publications

Enhanced 2-O-α-d-Glucopyranosyl-l-ascorbic Acid Synthesis through Iterative Saturation Mutagenesis of Acceptor Subsite Residues in Bacillus stearothermophilus NO2 Cyclodextrin Glycosyltransferase

Enhanced 2-O-α-d-Glucopyranosyl-l-ascorbic Acid Synthesis through Iterative Saturation Mutagenesis of Acceptor Subsite Residues in Bacillus stearothermophilus NO2 Cyclodextrin Glycosyltransferase

Maltooligosaccharides: Properties, Production and Applications

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

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