DOCSLIB.ORG

Expression of Different Glucansucrases in Potato Tubers: Implications for Starch Biosynthesis

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Expression of Different Glucansucrases in Potato Tubers: Implications for Starch Biosynthesis Expression of different glucansucrases in potato tubers: Implications for starch biosynthesis Géraldine Kok-Jacon Promotor : Prof. Dr. R.G.F. Visser Hoogleraar in de Plantenveredeling Co-promotor : Dr. Ir. J.-P. Vincken Universitair docent Laboratorium voor Plantenveredeling Promotiecommissie : Prof. Dr. Ir. E. Jacobsen, Wageningen Universiteit Prof. Dr. L.H.W. van der Plas, Wageningen Universiteit Prof. Dr. L. Dijkhuizen, Rijks Universiteit Groningen Dr. M. Quanz, Bayer Bioscience, Potsdam, Duitsland Dit onderzoek is uitgevoerd binnen de onderzoekschool Experimentele Planten Wetenschappen Expression of different glucansucrases in potato tubers: Implications for starch biosynthesis G.raldine Kok-Jacon Proefschrift ter verkrijging van de graad van doctor op gezag van de rector magnificus van Wageningen Universiteit, Prof. dr. M. J. Kropff, in het openbaar te verdedigen op maandag 19 september 2005 des namiddags te vier uur in de Aula. Expression of different glucansucrases in potato tubers: Implications for starch biosynthesis. Géraldine Kok-Jacon. Thesis Wageningen University, The Netherlands, 2005. With references - with summaries in English, Dutch and French. ISBN 90-8504-262-3 à Sjaak, Contents Chapter 1 General introduction 9 Chapter 2 Production of dextran in transgenic potato plants 33 Chapter 3 Mutan produced in potato amyloplasts adheres to starch granules 53 Chapter 4 Production of alternan in transgenic potato plants 73 Chapter 5 Granule-bound mutansucrase alters melting temperature of starch granules 87 Chapter 6 General discussion 107 Summary, Samenvatting, Résumé 117 Nawoord 129 Curriculum Vitae and Publications 131 9 : C hapter 1/ General introduction Towards a more versatile α-glucan biosynthesis in plants Géraldine A. Kok-Jacon Jean-Paul Vincken Qin Ji Richard G.F. Visser Graduate School Experimental Plant Sciences, Laboratory of Plant Breeding, Wageningen University, P.O. Box 386, 6700 AJ Wageningen, The Netherlands. Abstract : Starch is an important storage polysaccharide in many plants. It is composed of densely packed α-glucans, consisting of 1,4- and 1,4,6-linked glucose residues. The starch polymers are used in many industrial applications. The biosynthetic machinery for assembling the granule has been modified in many different ways in order to gain insight in the starch biosynthesis process, and to engineer starches with improved functionalities. With respect to the latter, two generic technologies with great potential are developed: (i) introduction of new linkage types in starch polymers (1,3- and 1,6-linkages), and (ii) engineering granule- boundness. The toolbox to engineer this new generation of starch polymers is discussed. Part of this Chapter was published in: Journal of Plant Physiology 160; 765-777 (2003). Reprinted with permission of Blackwell Publishing Key words: starch modification, glucansucrase, starch-binding domain, granule-boundness, transgenic potato 10 : Chapter 1/ General introduction Introduction During the last 10 years, the increased need for starches with novel properties has occupied the research community, and many efforts have concentrated on unraveling the starch biosynthesis pathways. The knowledge generated in these investigations was subsequently used to produce tailor-made starches in higher plants using recombinant DNA technology. Examples of starches with new functionalities are those with a modified degree of branching (Schwall et al. 2000; Shewmaker et al. 1994; Kortstee et al. 1996) and the amylose-free starch (Visser et al. 1991a; Kuipers et al. 1994), some of which hold potential for applications in the paper-, textile-, plastics-, food and pharmaceutical industry. The accumulation of more starch has also been an objective, but this will not be discussed further here (Slattery et al. 2000). In our laboratory, we have embarked on two generic technologies with a very wide range of applicability: (i) introduction of new linkage types and structural elements using glucansucrases, and (ii) engineering granule-boundness by using microbial starch- binding domains (SBDs). It is expected that these technologies will contribute significantly to the biosynthesis of more versatile α-glucans in the near future, leading to starches with improved functionalities that cannot be obtained by conventional breeding. In this paper, these recent developments in starch modification using heterologous expression of microbial genes will be reviewed, with emphasis on the potato crop. Starch structure and biosynthesis Starch is an important reserve carbohydrate found in many plant species, and is deposited as granules in the chloroplasts of green leaves (transitory starch) and in amyloplasts of tubers, roots and seeds (storage starch) (Kossmann and Lloyd 2000). Each starch granule has a highly organized structure defined by the succession of crystalline and amorphous lamellae (Fig. 1). The two main components of starch, amylopectin and amylose, are polymers of glucose. The major polysaccharide of the two, amylopectin (70-80%) is a highly branched molecule, mainly composed of α-1,4- linked glucosyl residues and 4-6% of α-1,4,6-linked branch points. The distribution of the branch points is not at random , enabling the unique, cluster-based structure of amylopectin (Thompson 2000). Clustering of the branch points in the amorphous lamellae enables the polymer chains to line up in a parallel fashion. The chains can 11 : Chapter 1/ General introduction Figure 1. Overview of the various l evels of polymer organization within the starch granule, which is composed of amylopectin and amylose molecules associate with each other to form double helices (Smith et al . 1997; Ball et al . 1998). This chain organization forms the basis of the semi-crystalline structure of the starch granule (Myers et al . 2000). In contrast to amylopectin, amylose (about 20-30%) is an essentially linear polysaccharide with less than 1% of branch points. In plant storage organs, starch biosynthesis takes place within the amyloplast (Fig. 2) and is the result of different reactions such as synthesis (polymerization of glucosyl residues), rearrangement and degradation, in which various starch synthases (E.C.2.4.1.21), transferases (branching (E.C.2.4.1.18) and disproportionating enzymes (E.C.2.4.1.25)), and hydrolytic enzymes (debranching enzyme (E.C.3.2.1.41)), respectively, play key roles. Sucrose is the starting point of starch biosynthesis, which is converted into hexose-phosphate sugars in the cytoplasm. In potato, glucose-6- phosphate (Glc-6P) is transported into the amyloplast (Kammerer et al. 1998). It is first converted to glucose-1-phosphate (Glc-1P) by plastidial phosphoglucomutase (PGM) (E.C.5.4.2.2) and, subsequently, to ADP-glucose (ADP-Glc) by ADP-glucose pyrophosphorylase (AGPase, E.C.2.7.7.27) (Tauberger et al . 2000; Müller-Röber et al . 1992; Stark et al . 1992). ADP-Glc serves as a substrate for the different starch synthase isoforms, some of which are mainly present in the soluble phase or stroma (SS-isoforms), while others are associated with the granule. The exclusively granule- 12 : Chapter 1/ General introduction Figure 2. Schematic representation of starch biosynthesis in a potato tuber cell. A: sucrose synthase (E.C.2.4.1.13); B: UDP-Glc pyrophosphorylase (E.C.2.7.7.9); C: phosphoglucomutase; D: Glc-6P isomerase (E.C.5.3.1.9); E: hexose kinase (E.C.2.7.1.1); F: plastidial phosphoglucomutase; G: ADP-Glc pyrophosphorylase; H: many enzymes such as starch synthase, branching enzymes, debranching enzymes, etc. ; I: non-native glucansucrases. Suc = sucrose, Glc = glucose; Frc = fructose. : translocators; 1: putative sucrose transporter; 2: G6PT (Glc-6P/Pi antiporter) (Kammerer et al. 1998); 3: putative hexose transporter related to the GLUT family (Weber et al . 2000); 4: putative sucrose transporter. : transport of solutes; : reaction catalyzed by enzymes. Dotted arrows indicate putative reactions in transformed tuber cells after introduction of a bacterial glucansucrase. bound starch synthase (GBSSI) catalyzes the formation of amylose (Kuipers et al. 1994). Furthermore, it was shown that GBSSI can also contribute to amylopectin synthesis in potato, pea and the unicellular alga, Chlamydomonas reinhardtii (Baba et al. 1987; Denyer et al. 1996; van de Wal et al . 1998). All starch synthases elongate glucan chains by transferring the glucose moiety of ADP-Glc to the non-reducing end of α-1,4 linked glucans. The branching enzymes (BE) cleave α-1,4 linkages and form α- 1,6 linkages. Schwall et al. (2000) showed that antisensing these enzymes in potato led to less branching of the forth-coming starch. Additional enzymes such as the disproportionating enzymes (D-enzyme) cleave and rejoin α-1,4 linkages in starch 13 : Chapter 1/ General introduction polymers and the debranching enzymes (DBE) hydrolyze the α-1,6 linkage at branch points. Figure 3. Schematic representation of the starch biosynthesis pathway. The timing of the biosynthesis process is as follows: the darker the background colour, the later the event takes place. The role of the various enzymes is described in detai l in the text. The starch biosynthesis process is summarized schematically in Fig. 3. The model shows clearly that amylopectin is synthesized first, and that amylose is formed later. Two possible mechanisms for amylose biosynthesis have been proposed: (i) the amylopectin-primed pathway, and (ii) the malto-oligosaccharides (MOS)-primed pathway (Mouille et al . 1996; Ball et al . 1998; van de Wal et al. 1998, 2000; Denyer et al. 1999;
Load more

Recommended publications
  • University of Groningen Mutational and Biochemical Analysis Of
    University of Groningen Mutational and biochemical analysis of Lactobacillus reuteri glucansucrase enzymes Meng, Xiangfeng IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2015 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Meng, X. (2015). Mutational and biochemical analysis of Lactobacillus reuteri glucansucrase enzymes. University of Groningen. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 24-09-2021 Chapter 1 General introduction: Tailor-made α-glucans by GH70 glucansucrase enzymes In preparation for submission 7 Chapter 1 Introduction Fossil resources are currently the major energy source and primary feedstock for the chemical industry. However, these resources are finite and unsustainable. At the same time, the widespread use of fossil resources causes severe environmental problems, including climate changes and air pollution.
    [Show full text]
  • Posters A.Pdf
    INVESTIGATING THE COUPLING MECHANISM IN THE E. COLI MULTIDRUG TRANSPORTER, MdfA, BY FLUORESCENCE SPECTROSCOPY N. Fluman, D. Cohen-Karni, E. Bibi Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel In bacteria, multidrug transporters couple the energetically favored import of protons to export of chemically-dissimilar drugs (substrates) from the cell. By this function, they render bacteria resistant against multiple drugs. In this work, fluorescence spectroscopy of purified protein is used to unravel the mechanism of coupling between protons and substrates in MdfA, an E. coli multidrug transporter. Intrinsic fluorescence of MdfA revealed that binding of an MdfA substrate, tetraphenylphosphonium (TPP), induced a conformational change in this transporter. The measured affinity of MdfA-TPP was increased in basic pH, raising a possibility that TPP might bind tighter to the deprotonated state of MdfA. Similar increases in affinity of TPP also occurred (1) in the presence of the substrate chloramphenicol, or (2) when MdfA is covalently labeled by the fluorophore monobromobimane at a putative chloramphenicol interacting site. We favor a mechanism by which basic pH, chloramphenicol binding, or labeling with monobromobimane, all induce a conformational change in MdfA, which results in deprotonation of the transporter and increase in the affinity of TPP. PHENOTYPE CHARACTERIZATION OF AZOSPIRILLUM BRASILENSE Sp7 ABC TRANSPORTER (wzm) MUTANT A. Lerner1,2, S. Burdman1, Y. Okon1,2 1Department of Plant Pathology and Microbiology, Faculty of Agricultural, Food and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot, Israel, 2The Otto Warburg Center for Agricultural Biotechnology, Faculty of Agricultural, Food and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot, Israel Azospirillum, a free-living nitrogen fixer, belongs to the plant growth promoting rhizobacteria (PGPR), living in close association with plant roots.
    [Show full text]
  • Structural Changes in the Oral Microbiome of the Adolescent
    www.nature.com/scientificreports OPEN Structural changes in the oral microbiome of the adolescent patients with moderate or severe dental fuorosis Qian Wang1,2, Xuelan Chen1,4, Huan Hu2, Xiaoyuan Wei3, Xiaofan Wang3, Zehui Peng4, Rui Ma4, Qian Zhao4, Jiangchao Zhao3*, Jianguo Liu1* & Feilong Deng1,2,3* Dental fuorosis is a very prevalent endemic disease. Although oral microbiome has been reported to correlate with diferent oral diseases, there appears to be an absence of research recognizing any relationship between the severity of dental fuorosis and the oral microbiome. To this end, we investigated the changes in oral microbial community structure and identifed bacterial species associated with moderate and severe dental fuorosis. Salivary samples of 42 individuals, assigned into Healthy (N = 9), Mild (N = 14) and Moderate/Severe (M&S, N = 19), were investigated using the V4 region of 16S rRNA gene. The oral microbial community structure based on Bray Curtis and Weighted Unifrac were signifcantly changed in the M&S group compared with both of Healthy and Mild. As the predominant phyla, Firmicutes and Bacteroidetes showed variation in the relative abundance among groups. The Firmicutes/Bacteroidetes (F/B) ratio was signifcantly higher in the M&S group. LEfSe analysis was used to identify diferentially represented taxa at the species level. Several genera such as Streptococcus mitis, Gemella parahaemolysans, Lactococcus lactis, and Fusobacterium nucleatum, were signifcantly more abundant in patients with moderate/severe dental fuorosis, while Prevotella melaninogenica and Schaalia odontolytica were enriched in the Healthy group. In conclusion, our study indicates oral microbiome shift in patients with moderate/severe dental fuorosis.
    [Show full text]
  • Flavonoid Glucodiversification with Engineered Sucrose-Active Enzymes Yannick Malbert
    Flavonoid glucodiversification with engineered sucrose-active enzymes Yannick Malbert To cite this version: Yannick Malbert. Flavonoid glucodiversification with engineered sucrose-active enzymes. Biotechnol- ogy. INSA de Toulouse, 2014. English. NNT : 2014ISAT0038. tel-01219406 HAL Id: tel-01219406 https://tel.archives-ouvertes.fr/tel-01219406 Submitted on 22 Oct 2015 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Last name: MALBERT First name: Yannick Title: Flavonoid glucodiversification with engineered sucrose-active enzymes Speciality: Ecological, Veterinary, Agronomic Sciences and Bioengineering, Field: Enzymatic and microbial engineering. Year: 2014 Number of pages: 257 Flavonoid glycosides are natural plant secondary metabolites exhibiting many physicochemical and biological properties. Glycosylation usually improves flavonoid solubility but access to flavonoid glycosides is limited by their low production levels in plants. In this thesis work, the focus was placed on the development of new glucodiversification routes of natural flavonoids by taking advantage of protein engineering. Two biochemically and structurally characterized recombinant transglucosylases, the amylosucrase from Neisseria polysaccharea and the α-(1→2) branching sucrase, a truncated form of the dextransucrase from L. Mesenteroides NRRL B-1299, were selected to attempt glucosylation of different flavonoids, synthesize new α-glucoside derivatives with original patterns of glucosylation and hopefully improved their water-solubility.
    [Show full text]
  • Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria Sacha A
    MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, Mar. 2006, p. 157–176 Vol. 70, No. 1 1092-2172/06/$08.00ϩ0 doi:10.1128/MMBR.70.1.157–176.2006 Copyright © 2006, American Society for Microbiology. All Rights Reserved. Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria Sacha A. F. T. van Hijum,1,2†* Slavko Kralj,1,2† Lukasz K. Ozimek,1,2 Lubbert Dijkhuizen,1,2 and Ineke G. H. van Geel-Schutten1,3 Centre for Carbohydrate Bioprocessing, TNO-University of Groningen,1 and Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen,2 9750 AA Haren, The Netherlands, and Innovative Ingredients and Products Department, TNO Quality of Life, Utrechtseweg 48 3704 HE Zeist, The Netherlands3 INTRODUCTION .......................................................................................................................................................157 NOMENCLATURE AND CLASSIFICATION OF SUCRASE ENZYMES ........................................................158 GLUCANSUCRASES .................................................................................................................................................158 Reactions Catalyzed and Glucan Product Synthesis .........................................................................................161 Glucan synthesis .................................................................................................................................................161 Acceptor reaction ................................................................................................................................................161
    [Show full text]
  • Crystal Structure of Glucansucrase from the Dental Caries
    5 Life Science PF Activity Report 2010 #28 Crystal Structure of Glucansucrase from the Dental Caries Glucansucrases are members of the glycoside hy- second sucrose binding site, namely, subsite +1 and Pathogen, Streptococcus Mutans drolase family 70, and catalyze the formation of glucan +2 (Fig. 1(b) and 1(c)). Trp517 provides the platform with various types of glucosidic linkages, (1-3), (1- for glycosyl-acceptor binding, whereas residues such 4) or (1-6) bonds, from sucrose via transglycosylation as Tyr430, Asn481, and Ser589 comprising subsite lucansucrases from Streptococcus mutans (GTF-SI) catalyze an essential factor in the pathogenesis of dental reactions. In the oral cavity, glucan synthesis by S. mu- +1 are conserved in glucansucrases but not in sugar- caries. Resolution of the GTF-SI structure confi rmed that the domain order of glucansucrase-SI was circularly tans involves three extracellular enzymes, GTF-I, GTF- cutting enzymes. Among these residues, the position Gpermuted compared with that of the well-known -amylase, which catalyses the breakdown of starch into sug- SI and GTF-S. GTF-I and GTF-SI synthesize mainly in- of Asp593 in GTF-SI is critical for glucansucrases that ars. Based on the structure of GTF-SI and a comparison of the amino acids of other glucansucrases, it was revealed soluble sticky glucan with (1-3) glycosidic linkages. We make insoluble and sticky glucan with (1-3) glycosidic that the position of Asp593 in glucansucrase-SI is the most critical point for the orientation of the acceptor sugar, and have used AR-NE3A and 5A beamlines to identify the linkages.
    [Show full text]
  • (Α1‹ →‹ 6) Linkage Specificity in Reuteransucrase Of
    www.nature.com/scientificreports OPEN Structural determinants of alternating (α1 → 4) and (α1 → 6) linkage specificity in Received: 03 June 2016 Accepted: 26 September 2016 reuteransucrase of Lactobacillus Published: 17 October 2016 reuteri Xiangfeng Meng1, Tjaard Pijning2, Justyna M. Dobruchowska1, Huifang Yin1, Gerrit J. Gerwig1 & Lubbert Dijkhuizen1 The glucansucrase GTFA of Lactobacillus reuteri 121 produces an α-glucan (reuteran) with a large amount of alternating (α1 → 4) and (α1 → 6) linkages. The mechanism of alternating linkage formation by this reuteransucrase has remained unclear. GTFO of the probiotic bacterium Lactobacillus reuteri ATCC 55730 shows a high sequence similarity (80%) with GTFA of L. reuteri 121; it also synthesizes an α-glucan with (α1 → 4) and (α1 → 6) linkages, but with a clearly different ratio compared to GTFA. In the present study, we show that residues in loop977 (970DGKGYKGA977) and helix α4 (1083VSLKGA1088) are main determinants for the linkage specificity difference between GTFO and GTFA, and hence are important for the synthesis of alternating (α1 → 4) and (α1 → 6) linkages in GTFA. More remote acceptor substrate binding sites (i.e.+3) are also involved in the determination of alternating linkage synthesis, as shown by structural analysis of the oligosaccharides produced using panose and maltotriose as acceptor substrate. Our data show that the amino acid residues at acceptor substrate binding sites (+1, +2, +3…) together form a distinct physicochemical micro-environment that determines the alternating (α1 → 4) and (α1 → 6) linkages synthesis in GTFA. Lactic acid bacteria (LAB) have been widely explored for the production of fermented food, due to their abil- ity of producing lactic acid and their generally recognized as safe (GRAS) status1.
    [Show full text]
  • The Microbiota-Produced N-Formyl Peptide Fmlf Promotes Obesity-Induced Glucose
    Page 1 of 230 Diabetes Title: The microbiota-produced N-formyl peptide fMLF promotes obesity-induced glucose intolerance Joshua Wollam1, Matthew Riopel1, Yong-Jiang Xu1,2, Andrew M. F. Johnson1, Jachelle M. Ofrecio1, Wei Ying1, Dalila El Ouarrat1, Luisa S. Chan3, Andrew W. Han3, Nadir A. Mahmood3, Caitlin N. Ryan3, Yun Sok Lee1, Jeramie D. Watrous1,2, Mahendra D. Chordia4, Dongfeng Pan4, Mohit Jain1,2, Jerrold M. Olefsky1 * Affiliations: 1 Division of Endocrinology & Metabolism, Department of Medicine, University of California, San Diego, La Jolla, California, USA. 2 Department of Pharmacology, University of California, San Diego, La Jolla, California, USA. 3 Second Genome, Inc., South San Francisco, California, USA. 4 Department of Radiology and Medical Imaging, University of Virginia, Charlottesville, VA, USA. * Correspondence to: 858-534-2230, [email protected] Word Count: 4749 Figures: 6 Supplemental Figures: 11 Supplemental Tables: 5 1 Diabetes Publish Ahead of Print, published online April 22, 2019 Diabetes Page 2 of 230 ABSTRACT The composition of the gastrointestinal (GI) microbiota and associated metabolites changes dramatically with diet and the development of obesity. Although many correlations have been described, specific mechanistic links between these changes and glucose homeostasis remain to be defined. Here we show that blood and intestinal levels of the microbiota-produced N-formyl peptide, formyl-methionyl-leucyl-phenylalanine (fMLF), are elevated in high fat diet (HFD)- induced obese mice. Genetic or pharmacological inhibition of the N-formyl peptide receptor Fpr1 leads to increased insulin levels and improved glucose tolerance, dependent upon glucagon- like peptide-1 (GLP-1). Obese Fpr1-knockout (Fpr1-KO) mice also display an altered microbiome, exemplifying the dynamic relationship between host metabolism and microbiota.
    [Show full text]
  • University of Groningen Engineering the Glucansucrase GTFR
    University of Groningen Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity Hellmuth, Hendrik; Wittrock, Sabine; Kralj, Slavko; Dijkhuizen, Lubbert; Hofer, Bernd; Seibel, Juergen; Seibel, Jürgen Published in: Biochemistry DOI: 10.1021/bi800563r IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2008 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Hellmuth, H., Wittrock, S., Kralj, S., Dijkhuizen, L., Hofer, B., Seibel, J., & Seibel, J. (2008). Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity: Toward tailor-made polymer and oligosaccharide products. Biochemistry, 47(25), 6678-6684. https://doi.org/10.1021/bi800563r Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal.
    [Show full text]
  • University of Groningen Engineering the Glucansucrase GTFR Enzyme Reaction and Glycosidic Bond Specificity Hellmuth, Hendrik; Wi
    University of Groningen Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity Hellmuth, Hendrik; Wittrock, Sabine; Kralj, Slavko; Dijkhuizen, Lubbert; Hofer, Bernd; Seibel, Juergen; Seibel, Jürgen Published in: Biochemistry DOI: 10.1021/bi800563r IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2008 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Hellmuth, H., Wittrock, S., Kralj, S., Dijkhuizen, L., Hofer, B., Seibel, J., & Seibel, J. (2008). Engineering the glucansucrase GTFR enzyme reaction and glycosidic bond specificity: Toward tailor-made polymer and oligosaccharide products. Biochemistry, 47(25), 6678-6684. https://doi.org/10.1021/bi800563r Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal.
    [Show full text]
  • Structures and Characteristics of Carbohydrates in Diets Fed to Pigs: a Review Diego M
    Navarro et al. Journal of Animal Science and Biotechnology (2019) 10:39 https://doi.org/10.1186/s40104-019-0345-6 REVIEW Open Access Structures and characteristics of carbohydrates in diets fed to pigs: a review Diego M. D. L. Navarro1, Jerubella J. Abelilla1 and Hans H. Stein1,2* Abstract The current paper reviews the content and variation of fiber fractions in feed ingredients commonly used in swine diets. Carbohydrates serve as the main source of energy in diets fed to pigs. Carbohydrates may be classified according to their degree of polymerization: monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Digestible carbohydrates include sugars, digestible starch, and glycogen that may be digested by enzymes secreted in the gastrointestinal tract of the pig. Non-digestible carbohydrates, also known as fiber, may be fermented by microbial populations along the gastrointestinal tract to synthesize short-chain fatty acids that may be absorbed and metabolized by the pig. These non-digestible carbohydrates include two disaccharides, oligosaccharides, resistant starch, and non-starch polysaccharides. The concentration and structure of non-digestible carbohydrates in diets fed to pigs depend on the type of feed ingredients that are included in the mixed diet. Cellulose, arabinoxylans, and mixed linked β-(1,3) (1,4)-D-glucans are the main cell wall polysaccharides in cereal grains, but vary in proportion and structure depending on the grain and tissue within the grain. Cell walls of oilseeds, oilseed meals, and pulse crops contain cellulose, pectic polysaccharides, lignin, and xyloglucans. Pulse crops and legumes also contain significant quantities of galacto-oligosaccharides including raffinose, stachyose, and verbascose.
    [Show full text]
  • Levan and Levansucrase-A Mini Review
    INTERNATIONAL JOURNAL OF SCIENTIFIC & TECHNOLOGY RESEARCH VOLUME 4, ISSUE 05, MAY 2015 ISSN 2277-8616 Levan And Levansucrase-A Mini Review Bruna Caroline Marques Goncalves, Cristiani Baldo, Maria Antonia Pedrine Colabone Celligoi Abstract: Levansucrase is a fructosyltranferase that synthesizes levan and present great biotechnological interest. It’s being widely used in therapeutic, food, cosmetic and pharmaceutical industries. Levansucrase is produced by many microorganisms such as the Bacillus subtilis Natto using the sucrose fermentation. In this mini-review we described some properties and functions of this important group of enzymes and the recent technologies used in the production and purification of levansucrase and levan. Index Terms: Levan, levansucrase, fermentation, sucrose ———————————————————— 1 INTRODUCTION This enzyme contributes 60% of the extracellular sucrase The levansucrase (EC 2.4.1.10) is the best characterized activity, but it catalyses neither fructose polymerization into fructosyltranferases and are synthesize by most microbial levan nor degradation of polyfructose such as levan or inulin. levans by transferring a β(2→1)-D-frutosyl residue to the Thus, this enzyme differs from the B. subtilis SacC, which acceptor molecule (sucrose or levan) [1]. The database showed levanase activity in addition to sucrose hydrolysis. “carbohydrate-active enzymes” (CAZY) grouped the microbial FOUET et al. [5] characterized the precursor form of Bacillus levansucrases into glycoside hydrolases 68 family (GH68) due subtilis levansucrase and identified 3 structural genes induced to be able to act in specific substrate and share two catalytic, by sucrose. One of them, sacB, codify extracellular often acidic residues, acting as a protons donor and nucleophile levansucrase and 4 of 5 recognized regulatory loci are able to or general base, respectively [2].
    [Show full text]