Review Paper PULLULANASE FUNCTIONS in STARCH
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Supplementary Information
doi: 10.1038/nature06269 SUPPLEMENTARY INFORMATION METAGENOMIC AND FUNCTIONAL ANALYSIS OF HINDGUT MICROBIOTA OF A WOOD FEEDING HIGHER TERMITE TABLE OF CONTENTS MATERIALS AND METHODS 2 • Glycoside hydrolase catalytic domains and carbohydrate binding modules used in searches that are not represented by Pfam HMMs 5 SUPPLEMENTARY TABLES • Table S1. Non-parametric diversity estimators 8 • Table S2. Estimates of gross community structure based on sequence composition binning, and conserved single copy gene phylogenies 8 • Table S3. Summary of numbers glycosyl hydrolases (GHs) and carbon-binding modules (CBMs) discovered in the P3 luminal microbiota 9 • Table S4. Summary of glycosyl hydrolases, their binning information, and activity screening results 13 • Table S5. Comparison of abundance of glycosyl hydrolases in different single organism genomes and metagenome datasets 17 • Table S6. Comparison of abundance of glycosyl hydrolases in different single organism genomes (continued) 20 • Table S7. Phylogenetic characterization of the termite gut metagenome sequence dataset, based on compositional phylogenetic analysis 23 • Table S8. Counts of genes classified to COGs corresponding to different hydrogenase families 24 • Table S9. Fe-only hydrogenases (COG4624, large subunit, C-terminal domain) identified in the P3 luminal microbiota. 25 • Table S10. Gene clusters overrepresented in termite P3 luminal microbiota versus soil, ocean and human gut metagenome datasets. 29 • Table S11. Operational taxonomic unit (OTU) representatives of 16S rRNA sequences obtained from the P3 luminal fluid of Nasutitermes spp. 30 SUPPLEMENTARY FIGURES • Fig. S1. Phylogenetic identification of termite host species 38 • Fig. S2. Accumulation curves of 16S rRNA genes obtained from the P3 luminal microbiota 39 • Fig. S3. Phylogenetic diversity of P3 luminal microbiota within the phylum Spirocheates 40 • Fig. -
Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications
Hindawi Publishing Corporation Enzyme Research Volume 2012, Article ID 921362, 14 pages doi:10.1155/2012/921362 Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications Siew Ling Hii,1 Joo Shun Tan,2 Tau Chuan Ling,3 and Arbakariya Bin Ariff4 1 Department of Chemical Engineering, Faculty of Engineering and Science, Universiti Tunku Abdul Rahman, 53300 Kuala Lumpur, Malaysia 2 Institute of Bioscience, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia 3 Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia 4 Department of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia Correspondence should be addressed to Arbakariya Bin Ariff, [email protected] Received 26 March 2012; Revised 12 June 2012; Accepted 12 June 2012 Academic Editor: Joaquim Cabral Copyright © 2012 Siew Ling Hii et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The use of pullulanase (EC 3.2.1.41) has recently been the subject of increased applications in starch-based industries especially those aimed for glucose production. Pullulanase, an important debranching enzyme, has been widely utilised to hydrolyse the α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides, which enables a complete and efficient conversion of the branched polysaccharides into small fermentable sugars during saccharification process. The industrial manufacturing of glucose involves two successive enzymatic steps: liquefaction, carried out after gelatinisation by the action of α- amylase; saccharification, which results in further transformation of maltodextrins into glucose. -
GRAS Notice 975, Maltogenic Alpha-Amylase Enzyme Preparation
GRAS Notice (GRN) No. 975 https://www.fda.gov/food/generally-recognized-safe-gras/gras-notice-inventory novozyme~ Rethink Tomorrow A Maltogenic Alpha-Amylase from Geobacillus stearothermophilus Produced by Bacillus licheniformis Janet Oesterling, Regulatory Affairs, Novozymes North America, Inc., USA October 2020 novozyme~ Reth in k Tomorrow PART 2 - IDENTITY, METHOD OF MANUFACTURE, SPECIFICATIONS AND PHYSICAL OR TECHNICAL EFFECT OF THE NOTIFIED SUBSTANCE ..................................................................... 4 2.1 IDENTITY OF THE NOTIFIED SUBSTANCE ................................................................................ 4 2.2 IDENTITY OF THE SOURCE ......................................................................................................... 4 2.2(a) Production Strain .................................................................................................. 4 2.2(b) Recipient Strain ..................................................................................................... 4 2.2(c) Maltogenic Alpha-Amylase Expression Plasmid ................................................... 5 2.2(d) Construction of the Recombinant Microorganism ................................................. 5 2.2(e) Stability of the Introduced Genetic Sequences .................................................... 5 2.2(f) Antibiotic Resistance Gene .................................................................................. 5 2.2(g) Absence of Production Organism in Product ...................................................... -
GRAS Notice 000099: Pullulan
United States Department of Agriculture Agricultural Marketing Service | National Organic Program Document Cover Sheet https://www.ams.usda.gov/rules-regulations/organic/national-list/petitioned Document Type: ☒ National List Petition or Petition Update A petition is a request to amend the USDA National Organic Program’s National List of Allowed and Prohibited Substances (National List). Any person may submit a petition to have a substance evaluated by the National Organic Standards Board (7 CFR 205.607(a)). Guidelines for submitting a petition are available in the NOP Handbook as NOP 3011, National List Petition Guidelines. Petitions are posted for the public on the NOP website for Petitioned Substances. ☐ Technical Report A technical report is developed in response to a petition to amend the National List. Reports are also developed to assist in the review of substances that are already on the National List. Technical reports are completed by third-party contractors and are available to the public on the NOP website for Petitioned Substances. Contractor names and dates completed are available in the report. January 31, 2018 National List Manager USDA/AMS/NOP, Standards Division 1400 Independence Ave. SW Room 2648-So., Ag Stop 0268 Washington, DC 20250-0268 RE: Petition to add Pullulan to the National List at §205.605(a) as an allowed nonsynthetic ingredient in tablets and capsules for dietary supplements labeled “made with organic (specified ingredients or food group(s)).” Dear National List Manager: The Organic Trade Association1 is -
Application A1204 Βeta-Amylase from Soybean (Glycine Max)
OFFICIAL 27 October 2020 [139-20] Supporting document 1 Risk and Technical assessment – Application A1204 Βeta-amylase from soybean (Glycine max) as a processing aid (enzyme) Executive summary The purpose of the application is to amend Schedule 18 – Processing Aids of the Australia New Zealand Food Standards Code (the Code) to include the enzyme beta-amylase (β- amylase) (EC 3.2.1.2) produced from soybeans (Glycine max). β-Amylase is proposed as a processing aid in starch processing for the production of maltose syrup. The evidence presented to support the proposed use of the enzyme provides adequate assurance that the enzyme, in the quantity and form proposed to be used, is technologically justified and has been demonstrated to be effective in achieving its stated purpose. The enzyme meets international identity and purity specifications. β-Amylase from soybean is derived from the edible parts of the Glycine max plant, for which a history of safe use over generations is well known. FSANZ considers that soybean β-amylase is unlikely to pose an allergenicity concern. Bioinformatic analysis identified a degree of amino acid sequence homology between β- amylase from soybean and an allergenic protein from wheat, but FSANZ does not consider β-amylase to be of allergenic concern in wheat allergic individuals given the likely very low exposure and that the enzyme is likely to be digested in the stomach like other dietary proteins. The WHO/IUIS Allergen Nomenclature Database lists seven soy proteins that are food allergens. β-amylase from soybean is not one of these seven allergenic soy proteins and is not an allergen to individuals with soybean food allergy. -
Characterization of Starch Debranching Enzymes of Maize Endosperm Afroza Rahman Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1998 Characterization of starch debranching enzymes of maize endosperm Afroza Rahman Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Rahman, Afroza, "Characterization of starch debranching enzymes of maize endosperm " (1998). Retrospective Theses and Dissertations. 12519. https://lib.dr.iastate.edu/rtd/12519 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. -
(12) United States Patent (10) Patent No.: US 9,689,046 B2 Mayall Et Al
USOO9689046B2 (12) United States Patent (10) Patent No.: US 9,689,046 B2 Mayall et al. (45) Date of Patent: Jun. 27, 2017 (54) SYSTEM AND METHODS FOR THE FOREIGN PATENT DOCUMENTS DETECTION OF MULTIPLE CHEMICAL WO O125472 A1 4/2001 COMPOUNDS WO O169245 A2 9, 2001 (71) Applicants: Robert Matthew Mayall, Calgary (CA); Emily Candice Hicks, Calgary OTHER PUBLICATIONS (CA); Margaret Mary-Flora Bebeselea, A. et al., “Electrochemical Degradation and Determina Renaud-Young, Calgary (CA); David tion of 4-Nitrophenol Using Multiple Pulsed Amperometry at Christopher Lloyd, Calgary (CA); Lisa Graphite Based Electrodes', Chem. Bull. “Politehnica” Univ. Kara Oberding, Calgary (CA); Iain (Timisoara), vol. 53(67), 1-2, 2008. Fraser Scotney George, Calgary (CA) Ben-Yoav. H. et al., “A whole cell electrochemical biosensor for water genotoxicity bio-detection”. Electrochimica Acta, 2009, 54(25), 6113-6118. (72) Inventors: Robert Matthew Mayall, Calgary Biran, I. et al., “On-line monitoring of gene expression'. Microbi (CA); Emily Candice Hicks, Calgary ology (Reading, England), 1999, 145 (Pt 8), 2129-2133. (CA); Margaret Mary-Flora Da Silva, P.S. et al., “Electrochemical Behavior of Hydroquinone Renaud-Young, Calgary (CA); David and Catechol at a Silsesquioxane-Modified Carbon Paste Elec trode'. J. Braz. Chem. Soc., vol. 24, No. 4, 695-699, 2013. Christopher Lloyd, Calgary (CA); Lisa Enache, T. A. & Oliveira-Brett, A. M., "Phenol and Para-Substituted Kara Oberding, Calgary (CA); Iain Phenols Electrochemical Oxidation Pathways”, Journal of Fraser Scotney George, Calgary (CA) Electroanalytical Chemistry, 2011, 1-35. Etesami, M. et al., “Electrooxidation of hydroquinone on simply prepared Au-Pt bimetallic nanoparticles'. Science China, Chem (73) Assignee: FREDSENSE TECHNOLOGIES istry, vol. -
Production of a Thermostable Pullulanase by a Thermus Sp
38 J. Jpn. Soc. Starch Sci., Vol. 34, No. 1, p. 38•`44 (1987)•l Production of a Thermostable Pullulanase by a Thermus sp. Nobuyuki NAKAMURA,* Nobuhiro SASHIHARA,** Hiromi NAGAYAMA and Koki HORIKOSHI*** Laboratory of Bacterial Metabolism, The Superbugs Project, Research Development Corporation of Japan (2-28-8, Honkomagome, Bunkyo-ku, Tokyo 113, Japan) (Received November 29, 1986) A moderate thermophile that produces a large amount of extracellular pullulanase was isolated from soil. The isolate (AMD-33), that grew at 37 to 74•Ž with an optimum at 65•Ž, was identified as a Thermus sp. strain. Maximal enzyme production was attained after 3 days shaking cultivation at 60•Ž on a medium composed of 1% pullulan, 2% gelatin, 0.1% K2HPO4, 0.03% MgSO4•E7H2O and 0.25% CaCO3. Pullulanase synthesis was enhanced by pullulan, soluble starch and dextrin as well as maltose but not at all by glucose. The enzyme, which was most active at pH 5.5-5.7 and 70 , was stabilized by Ca2+, and the optimum temperature for activity shifted to 75•Ž in the presence of 3mM CaCl2. Pullulanase (pullulan 6-glucanohydrolase, EC grow during the processes and interfere with 3. 2. 1. 41) is a debranching enzyme which the saccharification. Accordingly, active and specifically cleaves the ƒ¿-1, 6-glucosidic linkages thermostable amylolytic enzymes will be very in pullulan and amylopectin. This enzyme is important for the starch processing industry. commercially produced using bacteria1•`5) and Although some mesophilic and thermophilic is generally used in combination with several bacteria which produce significant amounts of amylases such as glucoamylases, ƒ¿-amylases, pullulanases have been reported, 8,11•`18) little is ƒÀ-amylases and maltooligosaccharides-forming known about the formation and biochemical enzymes for the production of glucose, maltose characteristics of pullulanases from Gram and some related starch conversion syrups, negative thermophiles except for the cell because it improves the saccharification rates associated enzyme from T. -
Potential and Utilization of Thermophiles and Thermostable Enzymes in Biorefining Pernilla Turner, Gashaw Mamo and Eva Nordberg Karlsson*
Microbial Cell Factories BioMed Central Review Open Access Potential and utilization of thermophiles and thermostable enzymes in biorefining Pernilla Turner, Gashaw Mamo and Eva Nordberg Karlsson* Address: Dept Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden Email: Pernilla Turner - [email protected]; Gashaw Mamo - [email protected]; Eva Nordberg Karlsson* - [email protected] * Corresponding author Published: 15 March 2007 Received: 4 January 2007 Accepted: 15 March 2007 Microbial Cell Factories 2007, 6:9 doi:10.1186/1475-2859-6-9 This article is available from: http://www.microbialcellfactories.com/content/6/1/9 © 2007 Turner et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract In today's world, there is an increasing trend towards the use of renewable, cheap and readily available biomass in the production of a wide variety of fine and bulk chemicals in different biorefineries. Biorefineries utilize the activities of microbial cells and their enzymes to convert biomass into target products. Many of these processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lowered risk of contamination. Thermophiles have often been proposed as sources of industrially relevant thermostable enzymes. Here we discuss existing and potential applications of thermophiles and thermostable enzymes with focus on conversion of carbohydrate containing raw materials. -
Genes for Degradation and Utilization of Uronic Acid-Containing Polysaccharides of a Marine Bacterium Catenovulum Sp
Genes for degradation and utilization of uronic acid-containing polysaccharides of a marine bacterium Catenovulum sp. CCB-QB4 Go Furusawa, Nor Azura Azami and Aik-Hong Teh Centre for Chemical Biology, Universiti Sains Malaysia, Bayan Lepas, Penang, Malaysia ABSTRACT Background. Oligosaccharides from polysaccharides containing uronic acids are known to have many useful bioactivities. Thus, polysaccharide lyases (PLs) and glycoside hydrolases (GHs) involved in producing the oligosaccharides have attracted interest in both medical and industrial settings. The numerous polysaccharide lyases and glycoside hydrolases involved in producing the oligosaccharides were isolated from soil and marine microorganisms. Our previous report demonstrated that an agar-degrading bacterium, Catenovulum sp. CCB-QB4, isolated from a coastal area of Penang, Malaysia, possessed 183 glycoside hydrolases and 43 polysaccharide lyases in the genome. We expected that the strain might degrade and use uronic acid-containing polysaccharides as a carbon source, indicating that the strain has a potential for a source of novel genes for degrading the polysaccharides. Methods. To confirm the expectation, the QB4 cells were cultured in artificial seawater media with uronic acid-containing polysaccharides, namely alginate, pectin (and saturated galacturonate), ulvan, and gellan gum, and the growth was observed. The genes involved in degradation and utilization of uronic acid-containing polysaccharides were explored in the QB4 genome using CAZy analysis and BlastP analysis. Results. The QB4 cells were capable of using these polysaccharides as a carbon source, and especially, the cells exhibited a robust growth in the presence of alginate. 28 PLs and 22 GHs related to the degradation of these polysaccharides were found in Submitted 5 August 2020 the QB4 genome based on the CAZy database. -
Long-Term Warming in a Mediterranean-Type Grassland Affects Soil Bacterial Functional Potential but Not Bacterial Taxonomic Composition
www.nature.com/npjbiofilms ARTICLE OPEN Long-term warming in a Mediterranean-type grassland affects soil bacterial functional potential but not bacterial taxonomic composition Ying Gao1,2, Junjun Ding2,3, Mengting Yuan4, Nona Chiariello5, Kathryn Docherty6, Chris Field 5, Qun Gao2, Baohua Gu 7, Jessica Gutknecht8,9, Bruce A. Hungate 10,11, Xavier Le Roux12, Audrey Niboyet13,14,QiQi2, Zhou Shi4, Jizhong Zhou2,4,15 and ✉ Yunfeng Yang2 Climate warming is known to impact ecosystem composition and functioning. However, it remains largely unclear how soil microbial communities respond to long-term, moderate warming. In this study, we used Illumina sequencing and microarrays (GeoChip 5.0) to analyze taxonomic and functional gene compositions of the soil microbial community after 14 years of warming (at 0.8–1.0 °C for 10 years and then 1.5–2.0 °C for 4 years) in a Californian grassland. Long-term warming had no detectable effect on the taxonomic composition of soil bacterial community, nor on any plant or abiotic soil variables. In contrast, functional gene compositions differed between warming and control for bacterial, archaeal, and fungal communities. Functional genes associated with labile carbon (C) degradation increased in relative abundance in the warming treatment, whereas those associated with recalcitrant C degradation decreased. A number of functional genes associated with nitrogen (N) cycling (e.g., denitrifying genes encoding nitrate-, nitrite-, and nitrous oxidereductases) decreased, whereas nifH gene encoding nitrogenase increased in the 1234567890():,; warming treatment. These results suggest that microbial functional potentials are more sensitive to long-term moderate warming than the taxonomic composition of microbial community. -
Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications
Hindawi Publishing Corporation Enzyme Research Volume 2012, Article ID 921362, 14 pages doi:10.1155/2012/921362 Review Article Pullulanase: Role in Starch Hydrolysis and Potential Industrial Applications Siew Ling Hii,1 Joo Shun Tan,2 Tau Chuan Ling,3 and Arbakariya Bin Ariff4 1 Department of Chemical Engineering, Faculty of Engineering and Science, Universiti Tunku Abdul Rahman, 53300 Kuala Lumpur, Malaysia 2 Institute of Bioscience, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia 3 Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia 4 Department of Bioprocess Technology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia Correspondence should be addressed to Arbakariya Bin Ariff, [email protected] Received 26 March 2012; Revised 12 June 2012; Accepted 12 June 2012 Academic Editor: Joaquim Cabral Copyright © 2012 Siew Ling Hii et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The use of pullulanase (EC 3.2.1.41) has recently been the subject of increased applications in starch-based industries especially those aimed for glucose production. Pullulanase, an important debranching enzyme, has been widely utilised to hydrolyse the α-1,6 glucosidic linkages in starch, amylopectin, pullulan, and related oligosaccharides, which enables a complete and efficient conversion of the branched polysaccharides into small fermentable sugars during saccharification process. The industrial manufacturing of glucose involves two successive enzymatic steps: liquefaction, carried out after gelatinisation by the action of α- amylase; saccharification, which results in further transformation of maltodextrins into glucose.