Biocatalytic production of novel glycolipids with cellodextrin phosphorylase

Tran, Hai Giang; Desmet, Tom; Saerens, Karen; Waegeman, Hendrik; Vandekerckhove, Stéphanie; D’hooghe, Matthias; Bogaert, Inge Van; Soetaert, Wim

doi:10.1016/j.biortech.2011.09.085

Cited by 21 publications

(17 citation statements)

References 13 publications

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“…Analysis of the sophorolipid by HPLC and data was similar as mentioned in previous reports, i.e., peaks between 4 and 7 min for the acidic sophorolipid, while 10 to 20 min as lactonic sophorolipid [12][13][14]. The peaks were compared with control as well as the data from the literature [2,4,6,[12][13][14]. The lactonic form was observed in C16 and C18 fatty acid chained sophorolipid.…”

Section: Hplc Analysis Of Sophorolipidsupporting

confidence: 68%

Tuning surface-active properties of bio-surfactant sophorolipids by varying fatty-acid chain lengths

Ahn

Morya

Kim

2016

Korean J. Chem. Eng.

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Sophorolipids are a kind of glycolipid-based bio-surfactant, and some known yeasts can produce them by utilizing plant oil at elevated glucose. In spite of a high production yield, sophorolipids have a limited industrial application, due to their narrow range of HLB (hydrophile -lipophile balance) value. These molecules have regained the attention of researchers and industrialists due to their surface properties and versatile applicability in herbal medicine and cosmetics. The bioactivity and surface properties of sophorolipids are mainly governed by chain length and type of the fatty acid. Therefore, the present study was designed to produce and characterize sophorolipids with varying fatty acid chain lengths. Surface-properties like critical micelle concentration of produced sophorolipids were varying from 43 to 62 (dyne/cm). Foamability, dispersion power, and detergence were found to be higher for short chained fatty acids than the longer ones. Cleaning ability of sophorolipid for FLUX coated PCB was found to be better than the chemical surfactants. Biodegradation rates of the sophorolipids were found to be higher than of the linear alkylbenzene sulfonate (LAS) at room temperature as well as 4 o C. These results showed that the properties of sophorolipids can be tuned by varying the chain' s properties of fatty acids, and it may be possible to customize the properties of sophorolipids for specific industrial applications.

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Section: Hplc Analysis Of Sophorolipidsupporting

confidence: 68%

Tuning surface-active properties of bio-surfactant sophorolipids by varying fatty-acid chain lengths

Ahn

Morya

Kim

2016

Korean J. Chem. Eng.

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“…[10] In a similar way, CDP-catalysed reactions provide access to b-1,4-glucanlinked, cellulose-like materials. [11,12] In terms of single sugar addition, as opposed to oligo/polymerisation reactions with its natural substrate Glc1P, CDP has been shown to be capable of using the anomeric phosphates of xylose (synthesis of a library of b-(1,4) hetero-oligosaccharides), [13] galactose (biocatalytic production of novel glycolipids) [14] and glucosamine (microscale reaction; preparative utility not demonstrated). [6] We recently identified algal and bacterial b-1,3-glucan phosphorylases (e.g., Pro_7066) that are capable of producing b-1,3-glucan…”

Section: Introductionmentioning

confidence: 99%

Preparative and Kinetic Analysis of β‐1,4‐ and β‐1,3‐Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof

et al. 2019

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The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of wild‐type cellodextrin phosphorylase (CDP: β‐1,4‐glucan linkage‐dependent) and laminaridextrin phosphorylase (Pro_7066: β‐1,3‐glucan linkage‐dependent) to tolerate a number of sugar‐1‐ phosphate substrates, albeit with reduced kinetic efficiency. In spite of catalytic efficiencies of <1 % of the natural reactions, we demonstrate the utility of given phosphorylase–sugar phosphate pairs to access new‐to‐nature fragments of human milk oligosaccharides, or analogues thereof, in multi‐milligram quantities.

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“…The majority of GH94 GPs use glucose 1‐phosphate (Glc1P) as a donor substrate, with the exception of chitobiose phosphorylase (ChBP), which uses α‐ N ‐acetyl‐ d ‐glucosamine 1‐phosphate (GlcNAc1P) as its natural donor, although it can also use Glc1P with 20 times reduction in efficiency . Relaxed donor specificity has also been demonstrated for CDP from R. stercorarium , which can use either Glc1P or α‐ d ‐galactose 1‐phosphate (Gal1P) as its glycosyl donor for glycolipid synthesis, albeit with ten times less efficiency on Gal1P . Both CBP and CDP from Ruminiclostridium thermocellum are capable of using α‐ d ‐glucosyl fluoride as a donor for the synthesis of cellobiose and cellodextrin …”

Section: Introductionmentioning

confidence: 99%

Unravelling the Specificity of Laminaribiose Phosphorylase from Paenibacillus sp. YM‐1 towards Donor Substrates Glucose/Mannose 1‐Phosphate by Using X‐ray Crystallography and Saturation Transfer Difference NMR Spectroscopy

et al. 2018

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Glycoside phosphorylases (GPs) carry out a reversible phosphorolysis of carbohydrates into oligosaccharide acceptors and the corresponding sugar 1-phosphates. The reversibility of the reaction enables the use of GPs as biocatalysts for carbohydrate synthesis. Glycosyl hydrolase family 94 (GH94), which only comprises GPs, is one of the most studied GP families that have been used as biocatalysts for carbohydrate synthesis, in academic research and in industrial production. Understanding the mechanism of GH94 enzymes is a crucial step towards enzyme engineering to improve and expand the applications of these enzymes in synthesis. In this work with a GH94 laminaribiose phosphorylase from Paenibacillus sp. YM-1 (PsLBP), we have demonstrated an enzymatic synthesis of disaccharide 1 (β-d-mannopyranosyl-(1→3)-d-glucopyranose) by using a natural acceptor glucose and noncognate donor substrate α-mannose 1-phosphate (Man1P). To investigate how the enzyme recognises different sugar 1-phosphates, the X-ray crystal structures of PsLBP in complex with Glc1P and Man1P have been solved, providing the first molecular detail of the recognition of a noncognate donor substrate by GPs, which revealed the importance of hydrogen bonding between the active site residues and hydroxy groups at C2, C4, and C6 of sugar 1-phosphates. Furthermore, we used saturation transfer difference NMR spectroscopy to support crystallographic studies on the sugar 1-phosphates, as well as to provide further insights into the PsLBP recognition of the acceptors and disaccharide products.

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Biocatalytic production of novel glycolipids with cellodextrin phosphorylase

Cited by 21 publications

References 13 publications

Tuning surface-active properties of bio-surfactant sophorolipids by varying fatty-acid chain lengths

Tuning surface-active properties of bio-surfactant sophorolipids by varying fatty-acid chain lengths

Preparative and Kinetic Analysis of β‐1,4‐ and β‐1,3‐Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof

Unravelling the Specificity of Laminaribiose Phosphorylase from Paenibacillus sp. YM‐1 towards Donor Substrates Glucose/Mannose 1‐Phosphate by Using X‐ray Crystallography and Saturation Transfer Difference NMR Spectroscopy

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