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Cellulases: Characteristics, Sources, Production, and Applications
8 CELLULASES: CHARACTERISTICS, SOURCES, PRODUCTION, AND APPLICATIONS Xiao-Zhou Zhang and Yi-Heng Percival Zhang 8.1 INTRODUCTION lulases: (1) endoglucanases (EC 3.2.1.4), (2) exogluca- nases, including cellobiohydrolases (CBHs) (EC Cellulose is the most abundant renewable biological 3.2.1.91), and (3) β -glucosidase (BG) (EC 3.2.1.21). To resource and a low-cost energy source based on energy hydrolyze and metabolize insoluble cellulose, the micro- content ($3–4/GJ) ( Lynd et al., 2008 ; Zhang, 2009 ). The organisms must secrete the cellulases (possibly except production of bio-based products and bioenergy from BG) that are either free or cell-surface-bound. Cellu- less costly renewable lignocellulosic materials would lases are increasingly being used for a large variety of bring benefi ts to the local economy, environment, and industrial purposes—in the textile industry, pulp and national energy security ( Zhang, 2008 ). paper industry, and food industry, as well as an additive High costs of cellulases are one of the largest obsta- in detergents and improving digestibility of animal cles for commercialization of biomass biorefi neries feeds. Now cellulases account for a signifi cant share of because a large amount of cellulase is consumed for the world ’ s industrial enzyme market. The growing con- biomass saccharifi cation, for example, ∼ 100 g enzymes cerns about depletion of crude oil and the emissions of per gallon of cellulosic ethanol produced ( Zhang et al., greenhouse gases have motivated the production of bio- 2006b ; Zhu et al., 2009 ). In order to decrease cellulase ethanol from lignocellulose, especially through enzy- use, increase volumetric productivity, and reduce capital matic hydrolysis of lignocelluloses materials—sugar investment, consolidated bioprocessing ( CBP ) has been platform ( Bayer et al., 2007 ; Himmel et al., 1999 ; Zaldi- proposed by integrating cellulase production, cellulose var et al., 2001 ). -
United States Patent (19) 11 Patent Number: 5,981,835 Austin-Phillips Et Al
USOO598.1835A United States Patent (19) 11 Patent Number: 5,981,835 Austin-Phillips et al. (45) Date of Patent: Nov. 9, 1999 54) TRANSGENIC PLANTS AS AN Brown and Atanassov (1985), Role of genetic background in ALTERNATIVE SOURCE OF Somatic embryogenesis in Medicago. Plant Cell Tissue LIGNOCELLULOSC-DEGRADING Organ Culture 4:107-114. ENZYMES Carrer et al. (1993), Kanamycin resistance as a Selectable marker for plastid transformation in tobacco. Mol. Gen. 75 Inventors: Sandra Austin-Phillips; Richard R. Genet. 241:49-56. Burgess, both of Madison; Thomas L. Castillo et al. (1994), Rapid production of fertile transgenic German, Hollandale; Thomas plants of Rye. Bio/Technology 12:1366–1371. Ziegelhoffer, Madison, all of Wis. Comai et al. (1990), Novel and useful properties of a chimeric plant promoter combining CaMV 35S and MAS 73 Assignee: Wisconsin Alumni Research elements. Plant Mol. Biol. 15:373-381. Foundation, Madison, Wis. Coughlan, M.P. (1988), Staining Techniques for the Detec tion of the Individual Components of Cellulolytic Enzyme 21 Appl. No.: 08/883,495 Systems. Methods in Enzymology 160:135-144. de Castro Silva Filho et al. (1996), Mitochondrial and 22 Filed: Jun. 26, 1997 chloroplast targeting Sequences in tandem modify protein import specificity in plant organelles. Plant Mol. Biol. Related U.S. Application Data 30:769-78O. 60 Provisional application No. 60/028,718, Oct. 17, 1996. Divne et al. (1994), The three-dimensional crystal structure 51 Int. Cl. ............................. C12N 15/82; C12N 5/04; of the catalytic core of cellobiohydrolase I from Tricho AO1H 5/00 derma reesei. Science 265:524-528. -
Synthesis and Structural Characterization of Glucooligosaccharides and Dextran from Weissella Confusa Dextransucrases
YEB Recent Publications in this Series Dextran from and and Structural Characterization of Glucooligosaccharides QIAO SHI Synthesis 4/2016 Hany S.M. EL Sayed Bashandy Flavonoid Metabolomics in Gerbera hybrida and Elucidation of Complexity in the Flavonoid Biosynthetic Pathway 5/2016 Erja Koivunen Home-Grown Grain Legumes in Poultry Diets 6/2016 Paul Mathijssen DISSERTATIONES SCHOLA DOCTORALIS SCIENTIAE CIRCUMIECTALIS, Holocene Carbon Dynamics and Atmospheric Radiative Forcing of Different Types of Peatlands ALIMENTARIAE, BIOLOGICAE. UNIVERSITATIS HELSINKIENSIS 21/2016 in Finland 7/2016 Seyed Abdollah Mousavi Revised Taxonomy of the Family Rhizobiaceae, and Phylogeny of Mesorhizobia Nodulating Glycyrrhiza spp. 8/2016 Sedeer El-Showk Auxin and Cytokinin Interactions Regulate Primary Vascular Patterning During Root QIAO SHI Development in Arabidopsis thaliana 9/2016 Satu Olkkola Antimicrobial Resistance and Its Mechanisms among Campylobacter coli and Campylobacter Synthesis and Structural Characterization of upsaliensis with a Special Focus on Streptomycin 10/2016 Windi Indra Muziasari Glucooligosaccharides and Dextran from Impact of Fish Farming on Antibiotic Resistome and Mobile Elements in Baltic Sea Sediment Weissella confusa Dextransucrases 11/2016 Kari Kylä-Nikkilä Genetic Engineering of Lactic Acid Bacteria to Produce Optically Pure Lactic Acid and to Develop a Novel Cell Immobilization Method Suitable for Industrial Fermentations 12/2016 Jane Etegeneng Besong epse Ndika Molecular Insights into a Putative Potyvirus RNA Encapsidation -
Transferable Step-Potentials For
© 2013 ANTHONY COFFMAN ALL RIGHTS RESERVED PRODUCTION OF CARBOHYDRASES BY FUNGUS TRICHODERMA REESEI GROWN ON SOY-BASED MEDIA A Thesis Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment of the Requirements for the Degree Master of Science Anthony Coffman December, 2013 PRODUCTION OF CARBOHYDRASES BY FUNGUS TRICHODERMA REESEI GROWN ON SOY-BASED MEDIA Anthony Coffman Thesis Approved: Accepted: ___________________________________ ___________________________________ Advisor Department Chair Dr. Lu-Kwang Ju Dr. Lu-Kwang Ju ___________________________________ ___________________________________ Committee Member Dean of The College Dr. Gang Cheng Dr. George K. Haritos ___________________________________ ___________________________________ Committee Member Dean of the Graduate School Dr. Chelsea N. Monty Dr. George R. Newkome ___________________________________ Date ii ABSTRACT Trichoderma reesei RUT-C30 was cultivated in shaker flasks and pH-controlled, agitated batch fermentations to study the effects of soy-based media on the production of cellulase, xylanase, and pectinase (polygalacturonase) for the purposes of soybean polysaccharide hydrolysis. Growth on defatted soybean flour as sole nitrogen source was compared to the standard combination of ammonium sulfate, proteose peptone, and urea. Carbon source effect was also examined for a variety of substrates, including lactose, microcrystalline cellulose (Avicel), citrus pectin, soy molasses, soy flour hydrolysate, and soybean hulls (both pretreated and natural). Flask study results indicated exceptional enzyme induction by Avicel and soybean hulls, while citrus pectin, soy molasses, and soy flour hydrolysate did not promote enzyme production. Batch fermentation experiments reflected the flask system results, showing the highest cellulase and xylanase activities for systems grown with Avicel and soybean hulls at near-neutral pH levels, and the highest polygalacturonase activity resulting from growth on lactose and soybean hulls at lower pH levels, 4.0 to 4.5. -
Cells of Commelina Communis1 Received for Publication April 8, 1987 and in Revised Form June 13, 1987 NINA L
Plant Physiol. (1987) 85, 360-364 0032-0889/87/85/0360/05/$01.00/0 Localization of Carbohydrate Metabolizing Enzymes in Guard Cells of Commelina communis1 Received for publication April 8, 1987 and in revised form June 13, 1987 NINA L. ROBINSON2 AND JACK PREISS*3 Department ofBiochemistry and Biophysics, University ofCalifornia, Davis, California 95616 ABSTRACI leaves. The sucrose is either degraded in the apoplast or in the cytoplasm of the storage cell. Sucrose, or its degradation prod- The lliztion ofenzymes involved in the flow of carbon into and out ucts, can be further metabolized to the triose-P or 3-PGA level. of starch was determined in guard cells of Commelina communis. The These compounds may then move into the amyloplast via the guard cell chloroplasts were separated from the rest of the cellular triose-P/Pi translocator and are converted into starch. However, components by a modification of published microfuge methods. The at present, the presence of the triose-P/Pi translocator in amy- enzymes of interest were then assayed in the supernatant and chloroplast loplasts has not been demonstrated. Assuming that the triose-P/ fractions. The chloroplast yield averaged 75% with 10% cytoplasmic Pi translocator is present, the movement of carbon into starch contamination. The enzymes involved in starch biosynthesis, ADPglucose would be a reversal of the enzymic steps occurring in the cyto- pyrophosphorylase, starch synthase, and branching enzyme, are located plasm with the last several steps resulting in the direct incorpo- exclusively in the chloroplast fraction. The enzymes involved in starch ration of carbon into starch. -
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. -
Xylooligosaccharides Production, Quantification, and Characterization
19 Xylooligosaccharides Production, Quantification, and Characterization in Context of Lignocellulosic Biomass Pretreatment Qing Qing1, Hongjia Li2,3,4,Ã, Rajeev Kumar2,4 and Charles E. Wyman2,3,4 1 Pharmaceutical Engineering & Life Science, Changzhou University, Changzhou, China 2 Center for Environmental Research and Technology, University of California, Riverside, USA 3 Department of Chemical and Environmental Engineering, University of California, Riverside, USA 4 BioEnergy Science Center, Oak Ridge, USA 19.1 Introduction 19.1.1 Definition of Oligosaccharides Oligosaccharides, also termed sugar oligomers, refer to short-chain polymers of monosaccharide units con- nected by a and/or b glycosidic bonds. In structure, oligosaccharides represent a class of carbohydrates between polysaccharides and monosaccharides, but the range of degree of polymerization (DP, chain length) spanned by oligosaccharides has not been consistently defined. For example, the Medical Subject Headings (MeSH) database of the US National Library of Medicine defines oligosaccharides as carbohy- drates consisting of 2–10 monosaccharide units; in other literature, sugar polymers with DPs of up to 30–40 have been included as oligosaccharides [1–3]. ÃPresent address: DuPont Industrial Biosciences, Palo Alto, USA Aqueous Pretreatment of Plant Biomass for Biological and Chemical Conversion to Fuels and Chemicals, First Edition. Edited by Charles E. Wyman. Ó 2013 John Wiley & Sons, Ltd. Published 2013 by John Wiley & Sons, Ltd. 392 Aqueous Pretreatment of Plant Biomass for -
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 -
How Liquorilactobacillus Hordei TMW 1.1822 Changes Its Behavior in the Presence of Sucrose in Comparison to Glucose
foods Article Living the Sweet Life: How Liquorilactobacillus hordei TMW 1.1822 Changes Its Behavior in the Presence of Sucrose in Comparison to Glucose Julia Bechtner 1 , Christina Ludwig 2, Michael Kiening 3, Frank Jakob 1 and Rudi F. Vogel 1,* 1 Lehrstuhl für Technische Mikrobiologie, Technische Universität München (TUM), 85354 Freising, Germany; [email protected] (J.B.); [email protected] (F.J.) 2 Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS), 85354 Freising, Germany; [email protected] 3 Lehrstuhl für Genomorientierte Bioinformatik, Technische Universität München (TUM), 85354 Freising, Germany; [email protected] * Correspondence: [email protected] Received: 2 August 2020; Accepted: 17 August 2020; Published: 21 August 2020 Abstract: Liquorilactobacillus (L.) hordei (formerly Lactobacillus hordei) is one of the dominating lactic acid bacteria within the water kefir consortium, being highly adapted to survive in this environment, while producing high molecular weight dextrans from sucrose. In this work, we extensively studied the physiological response of L. hordei TMW 1.1822 to sucrose compared to glucose, applying label-free, quantitative proteomics of cell lysates and exoproteomes. This revealed the differential expression of 53 proteins within cellular proteomes, mostly associated with carbohydrate uptake and metabolism. Supported by growth experiments, this suggests that L. hordei TMW 1.1822 favors fructose over other sugars. The dextransucrase was expressed irrespectively of the present carbon source, while it was significantly more released in the presence of sucrose (log2FC = 3.09), being among the most abundant proteins within exoproteomes of sucrose-treated cells. Still, L. hordei TMW 1.1822 expressed other sucrose active enzymes, predictively competing with the dextransucrase reaction. -
INVERTASE from SACCHAROMYCES CEREVISIAE
INVERTASE from SACCHAROMYCES CEREVISIAE New specifications prepared at the 57th JECFA (2001) and published in FNP 52 Add 9 (2001); previously prepared at the 15th JECFA (1971) as part of the specifications for “Carbohydrase from Saccharomyces species”, published in FNP 52. The use of this enzyme was considered to h be acceptable by the 57t JECFA (2001) if limited by Good Manufacturing Practice. SYNONYMS INS No. 1103 SOURCES Produced by the controlled submerged aerobic fermentation of a non- pathogenic and non-toxigenic strain of Saccharomyces cerevisiae and extracted from the yeast cells after washing and autolysis. Active principles β-Fructofuranosidase (synonym: invertase, carbohydrase, saccharase) Systematic names and β-Fructofuranosidase (EC 3.2.1.26; C.A.S. No. 9001-57-4) numbers Reactions catalysed Hydrolyses sucrose to yield glucose and fructose DESCRIPTION Typically white to tan amorphous powders or liquids that may be dispersed in food grade diluents and may contain stabilisers; soluble in water and practically insoluble in ethanol and ether. FUNCTIONAL USES Enzyme preparation Used in confectionery and pastry applications GENERAL Must conform to the General Specifications and Considerations for SPECIFICATIONS Enzyme Preparations Used in Food Processing (see Volume Introduction) CHARACTERISTICS IDENTIFICATION The sample shows invertase activity See description under TESTS TESTS Invertase activity Principle Invertase hydrolyses the non-reducing β-d-fructofuranoside residues of sucrose to yield invert sugar. The invert sugar released is then reacted with 3.5 dinitrosalicylic acid (DNS). The colour change produced is proportional to the amount of invert sugar released, which in turn is proportional to the invertase activity present in the sample. -
Invertase from Baker's Yeast (S
Invertase from baker's yeast (S. cerevisiae) Catalog Number I4504 Storage Temperature –20 °C CAS RN 9001-57-4 Reported KM values are 25 mM for sucrose and EC 3.2.1.26 150 mM for raffinose. At high substrate concentrations Synonyms: Saccharase, b-Fructofuranosidase, (1 M), invertase exhibits transferase activity by b-D-Fructofuranoside fructohydrolase transferring the b-D-fructofuranosyl residue to primary alcohols including ethanol, methanol, and n-propanol. Product Description Invertase does not require any activators and is Molecular mass:1 270 kDa inhibited by iodine, Zn2+, and Hg2+.1,3 Extinction coefficient:1 E1% = 23.0 (280 nm) pI:2 3.4–4.4 Precautions and Disclaimer This product is for R&D use only, not for drug, Invertase from baker's yeast is a glycoprotein household, or other uses. Please consult the Material containing 50% mannan and 2-3% glucosamine. During Safety Data Sheet for information regarding hazards purification, a small percentage of the enzyme may and safe handling practices. have part of the carbohydrate moiety removed leaving a heterogeneous enzyme with a lower or even negligible Preparation Instructions mannan content. This difference in carbohydrate This enzyme is soluble in water (10 mg/ml), yielding a content has led to the conclusion that two forms of the clear solution. enzyme exist. An external invertase (predominant form), carbohydrate containing, located outside of the References cell membrane and an internal invertase, which is 1. Lampen, J.O., The Enzymes, Boyer, P.D., ed., located entirely within the cytoplasm and devoid of any Academic Press (New York, NY:1971), carbohydrate.1,3 pp. -
Glucans with Potential Health Benefits Through Controlled Glucose Release in the Human
University of Groningen Synthesis of novel α-glucans with potential health benefits through controlled glucose release in the human gastrointestinal tract Gangoiti, Joana; Corwin, Sarah F; Lamothe, Lisa M; Vafiadi, Christina; Hamaker, Bruce R; Dijkhuizen, Lubbert Published in: Critical Reviews in Food Science and Nutrition DOI: 10.1080/10408398.2018.1516621 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: 2020 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Gangoiti, J., Corwin, S. F., Lamothe, L. M., Vafiadi, C., Hamaker, B. R., & Dijkhuizen, L. (2020). Synthesis of novel α-glucans with potential health benefits through controlled glucose release in the human gastrointestinal tract. Critical Reviews in Food Science and Nutrition, 60(1), 123-146. https://doi.org/10.1080/10408398.2018.1516621 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.