Application of Enzymes in Brewing
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Enzymes Handling/Processing
Enzymes Handling/Processing 1 Identification of Petitioned Substance 2 3 This Technical Report addresses enzymes used in used in food processing (handling), which are 4 traditionally derived from various biological sources that include microorganisms (i.e., fungi and 5 bacteria), plants, and animals. Approximately 19 enzyme types are used in organic food processing, from 6 at least 72 different sources (e.g., strains of bacteria) (ETA, 2004). In this Technical Report, information is 7 provided about animal, microbial, and plant-derived enzymes generally, and more detailed information 8 is presented for at least one model enzyme in each group. 9 10 Enzymes Derived from Animal Sources: 11 Commonly used animal-derived enzymes include animal lipase, bovine liver catalase, egg white 12 lysozyme, pancreatin, pepsin, rennet, and trypsin. The model enzyme is rennet. Additional details are 13 also provided for egg white lysozyme. 14 15 Chemical Name: Trade Name: 16 Rennet (animal-derived) Rennet 17 18 Other Names: CAS Number: 19 Bovine rennet 9001-98-3 20 Rennin 25 21 Chymosin 26 Other Codes: 22 Prorennin 27 Enzyme Commission number: 3.4.23.4 23 Rennase 28 24 29 30 31 Chemical Name: CAS Number: 32 Peptidoglycan N-acetylmuramoylhydrolase 9001-63-2 33 34 Other Name: Other Codes: 35 Muramidase Enzyme Commission number: 3.2.1.17 36 37 Trade Name: 38 Egg white lysozyme 39 40 Enzymes Derived from Plant Sources: 41 Commonly used plant-derived enzymes include bromelain, papain, chinitase, plant-derived phytases, and 42 ficin. The model enzyme is bromelain. -
Table S4. List of Enzymes Directly Involved in the Anti-Oxidant Defense Response
Table S4. List of Enzymes directly involved in the anti-oxidant defense response. Gene Name Gene Symbol Classification/Pathway 6-phosphogluconate dehydrogenase 6PGD NADPH regeneration/Pentose Phosphate Glucose-6-phosphate dehydrogenase G6PD NADPH regeneration/Pentose Phosphate Isocitrate Dehydrogenase 1 IDH1 NADPH regeneration/Krebs Isocitrate Dehydrogenase 2 IDH2 NADPH regeneration/Krebs Malic Enzyme 1 ME1 NADPH regeneration/Krebs Methylenetetrahydrofolate dehydrogenase 1 MTHFD1 NADPH regeneration/Folate Methylenetetrahydrofolate dehydrogenase 2 MTHFD2 NADPH regeneration/Folate Nicotinamide Nucleotide Transhydrogenase NNT NADPH regeneration/NAD Catalase CAT Antioxidants/Catalses/free radical detoxification Glutamate-cysteine ligase catalytic subunit GCLC Antioxidants/Glutathione synthesis Glutamate-cysteine ligase modifier subunit GCLM Antioxidants/Glutathione synthesis Glutathione peroxidase1 GPx1 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase2 GPx2 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase3 GPx3 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase4 GPx4 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase5 GPx5 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase6 GPx6 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione peroxidase7 GPx7 Antioxidants/Glutathione Peroxidases/free radical detoxification Glutathione S-transferase -
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 ). -
Application of Plant Proteolytic Enzymes for Tenderization of Rabbit Meat
Biotechnology in Animal Husbandry 34 (2), p 229-238 , 2018 ISSN 1450-9156 Publisher: Institute for Animal Husbandry, Belgrade-Zemun UDC 637.5.039'637.55'712 https://doi.org/10.2298/BAH1802229D APPLICATION OF PLANT PROTEOLYTIC ENZYMES FOR TENDERIZATION OF RABBIT MEAT Maria Doneva, Iliana Nacheva, Svetla Dyankova, Petya Metodieva, Daniela Miteva Institute of Cryobiology and Food Technology, Cherni Vrah 53, 1407, Sofia, Bulgaria Corresponding author: Maria Doneva, e-mail: [email protected] Original scientific paper Abstract: The purpose of this study is to assess the tenderizing effect of plant proteolytic enzymes upon raw rabbit meat. Tests are performed on rabbit meat samples treated with papain and two vegetal sources of natural proteases (extracts of kiwifruit and ginger root). Two variants of marinade solutions are prepared from each vegetable raw materials– 50% (w/w) and 100 % (w/w), with a duration of processing 2h, 24h, and 48h. Changes in the following physico- chemical characteristics of meat have been observed: pH, water-holding capacity, cooking losses and quantity of free amino acids. Differences in values of these characteristics have been observed, both between control and test samples, as well as depending of treatment duration. For meat samples marinated with papain and ginger extracts, the water-holding capacity reached to 6.74 ± 0.04 % (papain), 5.58 ± 0.09 % (variant 1) and 6.80 ± 0.11 % (variant 2) after 48 hours treatment. In rabbit meat marinated with kiwifruit extracts, a significant increase in WHC was observed at 48 hours, 3.37 ± 0.07 (variant 3) and 6.84 ± 0.11 (variant 4). -
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. -
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. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
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 -
Current IUBMB Recommendations on Enzyme Nomenclature and Kinetics$
Perspectives in Science (2014) 1,74–87 Available online at www.sciencedirect.com www.elsevier.com/locate/pisc REVIEW Current IUBMB recommendations on enzyme nomenclature and kinetics$ Athel Cornish-Bowden CNRS-BIP, 31 chemin Joseph-Aiguier, B.P. 71, 13402 Marseille Cedex 20, France Received 9 July 2013; accepted 6 November 2013; Available online 27 March 2014 KEYWORDS Abstract Enzyme kinetics; The International Union of Biochemistry (IUB, now IUBMB) prepared recommendations for Rate of reaction; describing the kinetic behaviour of enzymes in 1981. Despite the more than 30 years that have Enzyme passed since these have not subsequently been revised, though in various respects they do not nomenclature; adequately cover current needs. The IUBMB is also responsible for recommendations on the Enzyme classification naming and classification of enzymes. In contrast to the case of kinetics, these recommenda- tions are kept continuously up to date. & 2014 The Author. Published by Elsevier GmbH. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Contents Introduction...................................................................75 Kinetics introduction...........................................................75 Introduction to enzyme nomenclature ................................................76 Basic definitions ................................................................76 Rates of consumption and formation .................................................76 Rate of reaction .............................................................76 -
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. -
Fluoride Is a Strong and Specific Inhibitor of (~~Y~~E~R~C~~ Ap,A Hydrolases
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Volume 262, number 2, 205-208 FEBS 08241 March 1990 Fluoride is a strong and specific inhibitor of (~~y~~e~r~c~~ Ap,A hydrolases Andrzej Guranowski Katedra Biackemii, Ak~mia Rolnicza, ul. Wdyirska 35, PL-60-637 Poznati, Pala~d Received 24 November 1989; revised version received 19 January 1990 Fluoride acts as a noncompetitive, strong inhibitor of (usyrmnetricnf) Ap,A hydrolases (EC 361.17). The K, values estimated for the enzymes isolat- ed from seeds of some higher plants (yellow lupin, sunflower and marrow) are in the range of 2-3 pM and Is, for the hydrolase from a mammalian tissue (beef liver) is 20 BM. The anion, up to 25 mM, does not affect the following other enzymes which are able to degrade the bias’-n~l~sidyl~ oligophospha~s: Escherichiu coli (sym~tr~~ AphA hydrolase (EC 3.6.1.41), yeast Ap,A phosphorylsse (EC 2.7.7.53), yellow lupin Ap,A hydrol- ase (EC 3.6.1.29) and phosphodiesterase (EC 3.1.4.1). None of halogenic anions but fluoride affects the activity of (asynrmefricnf) Ap,A hydrolases. Usefulness of the fluoride effect for the in vivo studies on the Ap,A metabolism is shortly discussed. Fluoride; Enzyme inhibition; Ap,A hydrolase 1. INTRODUCTION of the dinucleotides catalyzed by lysyl-, phenylalanyl-, and alanyl-tRNA synthetases [2-51 and inhibits the rat Cellular levels of bis(5 ’ -nucleosidyl)oligophosphates [24] and lupin [l l] Ap3A hydrolases as well as the rat such as Ap.+A, Ap3A or Ap4G are probably modulated liver ApdA hydrolase f25]. -
Collection of Information on Enzymes a Great Deal of Additional Information on the European Union Is Available on the Internet
European Commission Collection of information on enzymes A great deal of additional information on the European Union is available on the Internet. It can be accessed through the Europa server (http://europa.eu.int). Luxembourg: Office for Official Publications of the European Communities, 2002 ISBN 92-894-4218-2 © European Communities, 2002 Reproduction is authorised provided the source is acknowledged. Final Report „Collection of Information on Enzymes“ Contract No B4-3040/2000/278245/MAR/E2 in co-operation between the Federal Environment Agency Austria Spittelauer Lände 5, A-1090 Vienna, http://www.ubavie.gv.at and the Inter-University Research Center for Technology, Work and Culture (IFF/IFZ) Schlögelgasse 2, A-8010 Graz, http://www.ifz.tu-graz.ac.at PROJECT TEAM (VIENNA / GRAZ) Werner Aberer c Maria Hahn a Manfred Klade b Uli Seebacher b Armin Spök (Co-ordinator Graz) b Karoline Wallner a Helmut Witzani (Co-ordinator Vienna) a a Austrian Federal Environmental Agency (UBA), Vienna b Inter-University Research Center for Technology, Work, and Culture - IFF/IFZ, Graz c University of Graz, Department of Dermatology, Division of Environmental Dermatology, Graz Executive Summary 5 EXECUTIVE SUMMARY Technical Aspects of Enzymes (Chapter 3) Application of enzymes (Section 3.2) Enzymes are applied in various areas of application, the most important ones are technical use, manufacturing of food and feedstuff, cosmetics, medicinal products and as tools for re- search and development. Enzymatic processes - usually carried out under mild conditions - are often replacing steps in traditional chemical processes which were carried out under harsh industrial environments (temperature, pressures, pH, chemicals). Technical enzymes are applied in detergents, for pulp and paper applications, in textile manufacturing, leather industry, for fuel production and for the production of pharmaceuticals and chiral substances in the chemical industry.