Oxidation of methyl α-d-galactopyranoside by galactose oxidase: products formed and optimization of reaction conditions for production of aldehyde

Parikka, Kirsti; Tenkanen, Maija

doi:10.1016/j.carres.2008.08.020

Cited by 73 publications

(101 citation statements)

References 29 publications

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“…was shown to target the C-6 position of galactose to produce aldehyde. The aldehyde was identified, using nuclear magnetic resonance, as a 6-ketal sugar (i.e., geminal diol) in water (38). Our hypothesis is supported by the MS/MS fragmentation patterns of the m/z 1,245 and the m/z 1,045 products that would correspond to triple oxidation for DP7 and double oxidation for DP6 at the reducing end, respectively ( Fig.…”

Section: Discussionsupporting

confidence: 57%

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Bey

Zhou

Poidevin

et al. 2013

Appl Environ Microbiol

159

151

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The genome of the coprophilic ascomycete Podospora anserina encodes 33 different genes encoding copper-dependent lytic polysaccharide monooxygenases (LPMOs) from glycoside hydrolase family 61 (GH61). In this study, two of these enzymes (P. anserina GH61A [PaGH61A] and PaGH61B), which both harbored a family 1 carbohydrate binding module, were successfully produced in Pichia pastoris. Synergistic cooperation between PaGH61A or PaGH61B with the cellobiose dehydrogenase (CDH) of Pycnoporus cinnabarinus on cellulose resulted in the formation of oxidized and nonoxidized cello-oligosaccharides. A striking difference between PaGH61A and PaGH61B was observed through the identification of the products, among which were doubly and triply oxidized cellodextrins, which were released only by the combination of PaGH61B with CDH. The mass spectrometry fragmentation patterns of these oxidized products could be consistent with oxidation at the C-6 position with a geminal diol group. The different properties of PaGH61A and PaGH61B and their effect on the interaction with CDH are discussed in regard to the proposed in vivo function of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.

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Section: Discussionsupporting

confidence: 57%

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Bey

Zhou

Poidevin

et al. 2013

Appl Environ Microbiol

159

151

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“…The main product in FgGaOx catalyzed reactions is a C-6 aldehyde (37). In aqueous solutions, the C-6 aldehydes exist as hydrates (geminal diols), and the doublet at 5.05 ppm was typical for the H-6Љ of the hydrate (37). A similar doublet was observed in the CgRaOx reaction (Fig.…”

Section: Fig 4 Kinetic Behavior Ofsupporting

confidence: 49%

“…5), confirming that the site of CgRaOx oxidation was the C-6 of the terminal galactose as well. Similarly to the FgGaOx catalyzed oxidation of methyl ␣-D-galactopyranoside (37), the doublet at 6.14 ppm corresponded to the olefinic hydrogen at C-4 of an ␣,␤-unsaturated C-6 aldehyde product (Fig. 5).…”

Section: Fig 4 Kinetic Behavior Ofmentioning

confidence: 99%

A Novel Colletotrichum graminicola Raffinose Oxidase in the AA5 Family

Andberg

Mollerup

Parikka

et al. 2017

Appl Environ Microbiol

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We describe here the identification and characterization of a copper radical oxidase from auxiliary activities family 5 (AA5_2) that was distinguished by showing preferential activity toward raffinose. Despite the biotechnological potential of carbohydrate oxidases from family AA5, very few members have been characterized. The gene encoding raffinose oxidase from Colletotrichum graminicola (CgRaOx; EC 1.1.3.Ϫ) was identified utilizing a bioinformatics approach based on the known modular structure of a characterized AA5_2 galactose oxidase. CgRaOx was expressed in Pichia pastoris, and the purified enzyme displayed the highest activity on the trisaccharide raffinose, whereas the activity on the disaccharide melibiose was three times lower and more than ten times lower activity was detected on D-galactose at a 300 mM substrate concentration. Thus, the substrate preference of CgRaOx was distinguished clearly from the substrate preferences of the known galactose oxidases. The site of oxidation for raffinose was studied by 1 H nuclear magnetic resonance and mass spectrometry, and we confirmed that the hydroxyl group at the C-6 position was oxidized to an aldehyde and that in addition uronic acid was produced as a side product. A new electrospray ionization mass spectrometry method for the identification of C-6 oxidized products was developed, and the formation mechanism of the uronic acid was studied. CgRaOx presented a novel activity pattern in the AA5 family.IMPORTANCE Currently, there are only a few characterized members of the CAZy AA5 protein family. These enzymes are interesting from an application point of view because of their ability to utilize the cheap and abundant oxidant O 2 without the requirement of complex cofactors such as FAD or NAD(P). Here, we present the identification and characterization of a novel AA5 member from Colletotrichum graminicola. As discussed in the present study, the bioinformatics approach using the modular structure of galactose oxidase was successful in finding a C-6 hydroxyl carbohydrate oxidase having substrate preference for the trisaccharide raffinose. By the discovery of this activity, the diversity of the CAZy AA5 family is increasing.KEYWORDS CAZy AA5, galactose oxidase, nuclear magnetic resonance, NMR, carbohydrate, EC 1.1.3.Ϫ E nzymes that cleave or form oligo-and polysaccharides are classified in the sequence-based carbohydrate-active enzyme database (CAZy [http://www.cazy .org]). The sequences are linked to information about functionality (e.g., substrate specificity) and three-dimensional structure. The CAZy database was recently expanded to account for redox enzymes, leading to the auxiliary activities (AA) group. Currently, 13 AA families exist, comprising lignolytic oxidoreductases (families AA1, -2, -4, and -6), lytic polysaccharide monooxygenases (families AA9, -10, -11, and -13), carbohydrate

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“…: depolymerization with carbohydrolases or lyases (Cheroni, Formantici, & Galante, 2010;Delattre et al, 2015;Tavernier et al, 2008), debranching with ␣-glycosidase, oxidation with oxidases (i.e., laccase, peroxidase, galactose oxidase), but also for the "elimination" of insoluble proteins with proteases (Baldaro et al, 2012). Enzymatic oxidation of guar GM has been described using either a wild type galactose oxidase (GaO), followed by reductive amination (Hall & Yalpani, 1980) or by halogen oxidation (Frollini, Reed, Milas, & Rinaudo, 1995), or with a highly engineered GaO by Parikka and co-workers (Delagrave et al, 2001(Delagrave et al, , 2002Ghafar et al, 2015;Leppanen et al, 2010;Mikkonen et al, 2014;Parikka & Tenkanen, 2009;Parikka et al, 2010Parikka et al, , 2012Parikka, Master, & Tenkanen, 2015). More generally, oxidation of polysaccharides with the enzyme laccase can generate reactive groups (e.g., carbonyls, carboxyls) on cellulose , on starch (Viikari, Niku-Paavola, et al, 1999), on pullulan (Jetten et al, 2000), and on guar galactomannan (Lavazza et al, 2011).…”

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confidence: 99%

An aerogel obtained from chemo-enzymatically oxidized fenugreek galactomannans as a versatile delivery system

Rossi

Campia

Merlini

et al. 2016

Carbohydrate Polymers

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a b s t r a c tWe describe a new aerogel obtained from laccase-oxidized galactomannans of the leguminous plant fenugreek (Trigonella foenum-graecum) and suggest its potential practical use.Laccase/TEMPO oxidation of fenugreek in aqueous solution caused a viscosity increase of over 15-fold. A structured, elastic, stable hydrogel was generated, due to formation of carbonyl groups from primary OH of galactose side units and subsequent establishment of hemiacetalic bonds with available free hydroxyl groups.Upon lyophilization of this hydrogel, a water-insoluble aerogel was obtained (EOLFG), capable of uptaking aqueous or organic solvents over 20 times its own weight. The material was characterized by scanning electron microscopy, FT-IR, elemental analysis and 13 C CP-MAS NMR spectroscopy and its mechanical properties were investigated.To test the EOLFG as a delivery system, the anti-microbial enzyme lysozyme was used as model active principle. Lysozyme was added before or after formation of the aerogel, entrapped or absorbed in the gel, retained and released in active form, as proven by its hydrolytic glycosidase activity on lyophilized Micrococcus lysodeikticus cells wall peptidoglycans.This new biomaterial, composed of a chemo-enzymatically modified plant polysaccharide, might represent a versatile, biocompatible "delivery system" of active principles in food and non-food products.

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Oxidation of methyl α-d-galactopyranoside by galactose oxidase: products formed and optimization of reaction conditions for production of aldehyde

Cited by 73 publications

References 29 publications

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina

A Novel Colletotrichum graminicola Raffinose Oxidase in the AA5 Family

An aerogel obtained from chemo-enzymatically oxidized fenugreek galactomannans as a versatile delivery system

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