Isomalto-oligosaccharides: Recent insights in production technology and their use for food and medical applications

Sorndech, Waraporn; Nakorn, Kuenchan Na; Tongta, Sunanta; Blennow, Andreas

doi:10.1016/j.lwt.2018.04.098

Cited by 69 publications

(48 citation statements)

References 47 publications

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“…The already proven relationship between food and health has promoted a growing biotechnological interest in functional foods and nutraceutical ingredient markets, where bioactive oligosaccharides are gaining relevance among compounds such as dietary fibres, peptides, polyols or unsaturated fatty acids [ 1 – 3 ]. Bioactive oligosaccharides include fructo-oligosaccharides (FOS), galacto-oligosaccharides (GOS), gluco-oligosaccharides (GlcOS), chito-oligosaccharides (COS) and xylo-oligosaccharides (XOS) among others [ 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and heterologous expression of two α-glucosidases from Metschnikowia spp, both producers of honey sugars

et al. 2020

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Background: α-Glucosidases are widely distributed enzymes with a varied substrate specificity that are traditionally used in biotechnological industries based on oligo-and polysaccharides as starting materials. According to amino acid sequence homology, α-glucosidases are included into two major families, GH13 and GH31. The members of family GH13 contain several α-glucosidases with confirmed hydrolytic activity on sucrose. Previously, a sucrose splitting activity from the nectar colonizing yeast Metschnikowia reukaufii which produced rare sugars with α-(1→1), α-(1→3) and α-(1→6) glycosidic linkages from sucrose was described. Results: In this study, genes codifying for α-glucosidases from the nectaries yeast M. gruessii and M. reukaufii were characterised and heterologously expressed in Escherichia coli for the first time. Recombinant proteins (Mg-αGlu and Mr-αGlu) were purified and biochemically analysed. Both enzymes mainly displayed hydrolytic activity towards sucrose, maltose and p-nitrophenyl-α-d-glucopyranoside. Structural analysis of these proteins allowed the identification of common features from the α-amylase family, in particular from glycoside hydrolases that belong to family GH13. The three acidic residues comprising the catalytic triad were identified and their relevance for the protein hydrolytic mechanism confirmed by site-directed mutagenesis. Recombinant enzymes produced oligosaccharides naturally present in honey employing sucrose as initial substrate and gave rise to mixtures with the same products profile (isomelezitose, trehalulose, erlose, melezitose, theanderose and esculose) previously obtained with M. reukaufii cell extracts. Furthermore, the same enzymatic activity was detected with its orthologous Mg-αGlu from M. gruessii. Interestingly, the isomelezitose amounts obtained in reactions mediated by the recombinant proteins, ~ 170 g/L, were the highest reported so far. Conclusions: Mg/Mr-αGlu were heterologously overproduced and their biochemical and structural characteristics analysed. The recombinant α-glucosidases displayed excellent properties in terms of mild reaction conditions, in addition to pH and thermal stability. Besides, the enzymes produced a rare mixture of hetero-gluco-oligosaccharides by transglucosylation, mainly isomelezitose and trehalulose. These compounds are natural constituents of honey which purification from this natural source is quite unviable, what make these enzymes very interesting for the

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Section: Introductionmentioning

confidence: 99%

Molecular characterization and heterologous expression of two α-glucosidases from Metschnikowia spp, both producers of honey sugars

et al. 2020

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“…Bioactive oligosaccharides are highly demanded products mainly for food and pharmaceutical industries, and their biotechnological production has increased in Asia, Europe and USA markets (Goffin et al , ; Sorndech et al , ). This sort of carbohydrates include lactulose, lactosucrose, soybean‐oligosaccharides, fructo‐oligosaccharides (FOS), galacto‐oligosaccharides (GOS) and xylo‐oligosaccharides (XOS), as well as gluco‐oligosaccharides (GlcOS) containing α‐(1→6) (isomalto‐oligosaccharides, IMOS), α‐(1→4), α‐(1→2) and α‐(1→3) linkages (Crittenden and Playne, ; Kim et al , ).…”

Section: Introductionmentioning

confidence: 99%

Efficient production of isomelezitose by a glucosyltransferase activity in Metschnikowia reukaufii cell extracts

García-González

Plou

Cervantes

et al. 2019

Microbial Biotechnology

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Summary Metschnikowia reukaufii is a widespread yeast able to grow in the plants’ floral nectaries, an environment of extreme conditions with sucrose concentrations exceeding 400 g l−1, which led us into the search for enzymatic activities involved in this sugar use/transformation. New oligosaccharides were produced by transglucosylation processes employing M. reukaufii cell extracts in overload‐sucrose reactions. These products were purified and structurally characterized by MS‐ESI and NMR techniques. The reaction mixture included new sugars showing a great variety of glycosidic bonds including α‐(1→1), α‐(1→3) and α‐(1→6) linkages. The main product synthesized was the trisaccharide isomelezitose, whose maximum concentration reached 81 g l−1, the highest amount reported for any unmodified enzyme or microbial extract. In addition, 51 g l−1 of the disaccharide trehalulose was also produced. Both sugars show potential nutraceutical and prebiotic properties. Interestingly, the sugar mixture obtained in the biosynthetic reactions also contained oligosaccharides such as esculose, a rare trisaccharide with no previous NMR structure elucidation, as well as erlose, melezitose and theanderose. All the sugars produced are naturally found in honey. These compounds are of biotechnological interest due to their potential food, cosmeceutical and pharmaceutical applications.

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“…IMOs are commonly produced from starch via enzymatic conversion using α-amylase, β-amylase, pullulanase and transglucosidase [11]. The typical process for IMO production usually comprises three steps: (1) liquefaction, where starch is liquefied by a thermostable α-amylase to produce dextrin; (2) saccharification, where the dextrin is then saccharified by β-amylase and pullulanase; (3) transglycosylation, where α-glucosidase is used for converting maltose (saccharified products) into IMOs [12]. Since commercial α-amylase, β-amylase and pullulanase are well-studied and their industrial uses are relatively mature, studying the transglycosylation reaction catalyzed by α-glucosidase is the key step in IMO production.…”

Section: Introductionmentioning

confidence: 99%

Heterologous Expression of a Thermostable α-Glucosidase from Geobacillus sp. Strain HTA-462 by Escherichia coli and Its Potential Application for Isomaltose–Oligosaccharide Synthesis

et al. 2019

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Isomaltose–oligosaccharides (IMOs), as food ingredients with prebiotic functionality, can be prepared via enzymatic synthesis using α-glucosidase. In the present study, the α-glucosidase (GSJ) from Geobacillus sp. strain HTA-462 was cloned and expressed in Escherichia coli BL21 (DE3). Recombinant GSJ was purified and biochemically characterized. The optimum temperature condition of the recombinant enzyme was 65 °C, and the half-life was 84 h at 60 °C, whereas the enzyme was active over the range of pH 6.0–10.0 with maximal activity at pH 7.0. The α-glucosidase activity in shake flasks reached 107.9 U/mL and using 4-Nitrophenyl β-D-glucopyranoside (pNPG) as substrate, the Km and Vmax values were 2.321 mM and 306.3 U/mg, respectively. The divalent ions Mn2+ and Ca2+ could improve GSJ activity by 32.1% and 13.8%. Moreover, the hydrolysis ability of recombinant α-glucosidase was almost the same as that of the commercial α-glucosidase (Bacillus stearothermophilus). In terms of the transglycosylation reaction, with 30% maltose syrup under the condition of 60 °C and pH 7.0, IMOs were synthesized with a conversion rate of 37%. These studies lay the basis for the industrial application of recombinant α-glucosidase.

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Isomalto-oligosaccharides: Recent insights in production technology and their use for food and medical applications

Cited by 69 publications

References 47 publications

Molecular characterization and heterologous expression of two α-glucosidases from Metschnikowia spp, both producers of honey sugars

Molecular characterization and heterologous expression of two α-glucosidases from Metschnikowia spp, both producers of honey sugars

Efficient production of isomelezitose by a glucosyltransferase activity in Metschnikowia reukaufii cell extracts

Heterologous Expression of a Thermostable α-Glucosidase from Geobacillus sp. Strain HTA-462 by Escherichia coli and Its Potential Application for Isomaltose–Oligosaccharide Synthesis

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