An Enzyme Composition for Combined Biopolishing and Bleach Clean-Up
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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). -
Helical Domain That Prevents Access to the Substrate-Binding Cleft
View metadata, citation and similar papers at core.ac.uk brought to you by CORE Researchprovided Article by Elsevier1193 - Publisher Connector The prosequence of procaricain forms an a-helical domain that prevents access to the substrate-binding cleft Matthew R Groves, Mark AJ Taylor, Mandy Scott, Nicola J Cummings Richard W Pickersgill* and John A Jenkins* Background: Cysteine proteases are involved in a variety of cellular processes Address: Department of Food Macromolecular including cartilage degradation in arthritis, the progression of Alzheimer’s Science, Institute of Food Research, Earley Gate, disease and cancer invasion: these enzymes are therefore of immense biological Whiteknights Road, Reading, RG6 6BZ, UK. importance. Caricain is the most basic of the cysteine proteases found in the *Corresponding authors. latex of Carica papaya. It is a member of the papain superfamily and is E-mail: [email protected] homologous to other plant and animal cysteine proteases. Caricain is naturally [email protected] expressed as an inactive zymogen called procaricain. The inactive form of the Key words: caricain, cysteine protease, density protease contains an inhibitory proregion which consists of an additional 106 modification, X-ray structure, zymogen N-terminal amino acids; the proregion is removed upon activation. Received: 25 June 1996 Results: The crystal structure of procaricain has been refined to 3.2 Å Revisions requested: 23 July 1996 Revisions received: 12 August 1996 resolution; the final model consists of three non-crystallographically related Accepted: 28 August 1996 molecules. The proregion of caricain forms a separate globular domain which binds to the C-terminal domain of mature caricain. -
Processing of Progranulin Into Granulins Involves Multiple Lysosomal Proteases and Is Affected in Frontotemporal Lobar Degeneration
Processing of progranulin into granulins involves multiple lysosomal proteases and is affected in frontotemporal lobar degeneration Swetha Mohan University of California San Francisco Paul J. Sampognaro University of California San Francisco Andrea R. Argouarch University of California San Francisco Jason C. Maynard University of California San Francisco Anand Patwardhan University of California San Francisco Emma C. Courtney University of California San Francisco Amanda Mason University of California San Francisco Kathy H. Li University of California San Francisco William W. Seeley University of California San Francisco Bruce L. Miller University of California San Francisco Alma Burlingame University of California San Francisco Mathew P. Jacobson University of California San Francisco Aimee Kao ( [email protected] ) University of California San Francisco https://orcid.org/0000-0002-7686-7968 Research article Keywords: Progranulin, granulin, frontotemporal lobar degeneration, lysosome, protease, pH, asparagine endopeptidase Page 1/31 Posted Date: July 29th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-44128/v2 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Version of Record: A version of this preprint was published at Molecular Neurodegeneration on August 3rd, 2021. See the published version at https://doi.org/10.1186/s13024-021-00472-1. Page 2/31 Abstract Background - Progranulin loss-of-function mutations are linked to frontotemporal lobar degeneration with TDP-43 positive inclusions (FTLD-TDP-Pgrn). Progranulin (PGRN) is an intracellular and secreted pro- protein that is proteolytically cleaved into individual granulin peptides, which are increasingly thought to contribute to FTLD-TDP-Pgrn disease pathophysiology. Intracellular PGRN is processed into granulins in the endo-lysosomal compartments. -
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. -
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 -
Esomeprazole Inhibits the Lysosomal Cysteine Protease Legumain to Prevent Cancer Metastasis
Investigational New Drugs https://doi.org/10.1007/s10637-020-01011-3 PRECLINICAL STUDIES Esomeprazole inhibits the lysosomal cysteine protease legumain to prevent cancer metastasis Tian Zhao1 & Yujie Liu1 & Yanfei Hao1 & Wei Zhang1 & Li Tao1 & Dong Wang1 & Yuyin Li1 & Zhenxing Liu1 & Edward A McKenzie2 & Qing Zhao1 & Aipo Diao1 Received: 17 August 2020 /Accepted: 21 September 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020 Summary Legumain is a newly discovered lysosomal cysteine protease that can cleave asparagine bonds and plays crucial roles in regulating immunity and cancer metastasis. Legumain has been shown to be highly expressed in various solid tumors, within the tumor microenvironment and its levels are directly related to tumor metastasis and poor prognosis. Therefore, legumain presents as a potential cancer therapeutic drug target. In this study, we have identified esomeprazole and omeprazole as novel legumain small molecule inhibitors by screening an FDA approved-drug library. These compounds inhibited enzyme activity of both recombinant and endog- enous legumain proteins with esomeprazole displaying the highest inhibitory effect. Further molecular docking analysis also indicated that esomeprazole, the S- form of omeprazole had the most stable binding to legumain protein compared to R-omeprazole. Transwell assay data showed that esomeprazole and omeprazole reduced MDA-MB-231 breast cancer cell invasion without effecting cell viability. Moreover, an in vivo orthotopic transplantation nude mouse model study showed that esomeprazole reduced lung metastasis of MDA-MB-231 breast cancer cells. These results indicated that esomeprazole has the exciting potential to be used in anti-cancer therapy by preventing cancer metastasis via the inhibition of legumain enzyme activity. -
Immobilization of Trypsin for Peptide Synthesis and Hydrolysis Reactions
IMMOBILIZATION OF TRYPSIN FOR PEPTIDE SYNTHESIS AND HYDROLYSIS REACTIONS zur Erlangung des akademischen Grades eines DOKTORS DER INGENIEURWISSENSCHAFTEN (Dr.-Ing.) der Fakultät für Chemieingenieurwesen und Verfahrenstechnik des Karlsruher Instituts für Technologie (KIT) vorgelegte genehmigte DISSERTATION von Dipl. Biol. (t.o.) Julia Andre geb. Stolarow aus Odessa, Ukraine Referent: Prof. Dr. rer. nat. Christoph Syldatk Korreferent: Prof. Dr.-Ing. Rudolf Hausmann Tag der mündlichen Prüfung: 19. November 2015 Maybe I will be something that you would be good at Für meine Eltern Acknowledgements I wish to express my sincere thanks to people who continuously supported and guided me throughout my work. Prof. Dr. rer. nat. Christoph Syldatk for giving me the opportunity to conduct my research work at his group, his guidance and his enormous scientific knowledge giving me a great opportunity to learn. Prof. Dr.-Ing. Rudolf Hausmann for his supervision, productive scientific discussions, his motivating personality and professional advice helping me to overcome many obstacles in my research work. Former and current members of the Technical Biology group for the great friendly and supporting atmosphere during my work and spare time: Dr.-Ing. Ines Schulze, Dr. rer. nat. Mareike Perzborn, Laura Krämer, Dr.-Ing. Berna Gerçe, Dr.-Ing. Martin Pöhnlein, Dipl.-Ing. Melanie Gerlitzki, Dipl.-Biotechnol. Johannes Kügler, Dr.-Ing. Marius Henkel, Dr. rer. nat. Markus Andre, Dr.-Ing. Ulrike Engel, M. Sc. Janina Beuker, Dipl.-Ing. Michaela Zwick, M. Sc. Judit Willenbacher, M. Sc. Sarah Dold, M. Sc. Christin Slomka, Sandra Baumann, Dr.-Ing. Katrin Ochsenreither, Dipl.-Ing. Florian Oswald, Desiree Westermann, Werner Mandel, Harald Gotzmann, Siegfried Almstedt, Katja Rupp, Susanne Warth, M. -
Evaluation of Ficain Activity in Different Fruit Samples of Ficus Carica Linn
Volume 5, Issue 10, October – 2020 International Journal of Innovative Science and Research Technology ISSN No:-2456-2165 Evaluation of Ficain Activity in Different Fruit Samples of Ficus carica Linn N.Ranjini, Kusuma.K, Srilakshmi.S, Sharu Raj K M* Department of PG studies in Biotechnology, Government Science College (Autonomous) Bengaluru-560001 Abstract:- Protease enzymes have increased commercial containing 5mM EDTA and 5mM cysteine was added and applications, but there are limited available known freeze dried. natural sources of these enzymes. This study was done to identify other sources of proteases, for which different 2.3. Qualitative analysis: stages of fig fruits (raw, ripened, and dry) were used, as Qualitative test for protein they are known sources of ficain enzyme. Ficain To identify the crude extract of (raw, ripened, dry) extracted from different fruit samples (raw, ripened,and fruit samples of Ficus carica L.as protein, some qualitative dry) was partially purified by chromatography on test were carried out such as Ninhydrin test and DEAE-cellulose. Caseinolytic activity studies were also Xanthoprotein test. This test gives color reactions on the carried out on the enzyme sample. Extraction of ficain basis of amino acid present in them. (Deb A C, 1996). from fig fruits is a novel approach. 2.4. Caseinolytic assay: Keywords:- Ficain, Fig Fruit, Protease, DEAE-Cellulose, Assay was carried out to determine the enzyme Caseinolytic. activity, by using casein as a substrate. 2% casein was prepared by using 1% sodium hydroxide solution. The I. INTRODUCTION reaction was carried out on 0.25ml of enzyme with 0.2ml of 2% casein. -
Chapter 11 Cysteine Proteases
CHAPTER 11 CYSTEINE PROTEASES ZBIGNIEW GRZONKA, FRANCISZEK KASPRZYKOWSKI AND WIESŁAW WICZK∗ Faculty of Chemistry, University of Gdansk,´ Poland ∗[email protected] 1. INTRODUCTION Cysteine proteases (CPs) are present in all living organisms. More than twenty families of cysteine proteases have been described (Barrett, 1994) many of which (e.g. papain, bromelain, ficain , animal cathepsins) are of industrial impor- tance. Recently, cysteine proteases, in particular lysosomal cathepsins, have attracted the interest of the pharmaceutical industry (Leung-Toung et al., 2002). Cathepsins are promising drug targets for many diseases such as osteoporosis, rheumatoid arthritis, arteriosclerosis, cancer, and inflammatory and autoimmune diseases. Caspases, another group of CPs, are important elements of the apoptotic machinery that regulates programmed cell death (Denault and Salvesen, 2002). Comprehensive information on CPs can be found in many excellent books and reviews (Barrett et al., 1998; Bordusa, 2002; Drauz and Waldmann, 2002; Lecaille et al., 2002; McGrath, 1999; Otto and Schirmeister, 1997). 2. STRUCTURE AND FUNCTION 2.1. Classification and Evolution Cysteine proteases (EC.3.4.22) are proteins of molecular mass about 21-30 kDa. They catalyse the hydrolysis of peptide, amide, ester, thiol ester and thiono ester bonds. The CP family can be subdivided into exopeptidases (e.g. cathepsin X, carboxypeptidase B) and endopeptidases (papain, bromelain, ficain, cathepsins). Exopeptidases cleave the peptide bond proximal to the amino or carboxy termini of the substrate, whereas endopeptidases cleave peptide bonds distant from the N- or C-termini. Cysteine proteases are divided into five clans: CA (papain-like enzymes), 181 J. Polaina and A.P. MacCabe (eds.), Industrial Enzymes, 181–195. -
^ P X R, for the PURPOSES of INFORMATION ONLY
WORLD INTELLECTUAL PROPERTY ORGANIZATION PCT International Bureau INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (51) International Patent Classification 6 : (11) International Publication Number: WO 98/49190 C07K 5/06, 5/08, 5/10 A l (43) International Publication Date: 5 November 1998 (05.11.98) (21) International Application Number: PCT/US98/08259 (74) Agents: BURKE, John, E. et al.; Cushman Darby & Cushman, Intellectual Property Group of Pillsbury Madison & Sutro, (22) International Filing Date: 24 April 1998 (24.04.98) 1100 New York Avenue, N.W., Washington, DC 20005 (US). (30) Priority Data: 60/044,819 25 April 1997 (25.04.97) US (81) Designated States: AL, AM, AT, AU, AZ, BA, BB, BG, BR, Not furnished 23 April 1998 (23.04.98) US BY, CA, CH, CN, CU, CZ, DE, DK, EE, ES, FI, GB, GE, GH, GM, GW, HU, ID, IL, IS, JP, KE, KG, KP, KR, KZ, LC, LK, LR, LS, LT, LU, LV, MD, MG, MK, MN, MW, (71) Applicant (for all designated States except US): CORTECH, MX, NO, NZ, PL, PT, RO, RU, SD, SE, SG, SI, SK, SL, INC. [US/US]; 6850 North Broadway, Denver, CO 80221 TJ, TM, TR, TT, UA, UG, US, UZ, VN, YU, ZW, ARIPO (US). patent (GH, GM, KE, LS, MW, SD, SZ, UG, ZW), Eurasian patent (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM), European (72) Inventors; and patent (AT, BE, CH, CY, DE, DK, ES, FI, FR, GB, GR, (75) Inventors/Applicants(for US only): SPRUCE, Lyle, W. IE, IT, LU, MC, NL, PT, SE), OAPI patent (BF, BJ, CF, [US/US]; 948 Camino Del Sol, Chula Vista, CA 91910 CG, Cl, CM, GA, GN, ML, MR, NE, SN, TD, TG). -
EUROPEAN COMMISSION Brussels, 28 April 2020 REGISTER of FOOD
EUROPEAN COMMISSION DIRECTORATE-GENERAL FOR HEALTH AND FOOD SAFETY Food and feed safety, innovation Food processing technologies and novel foods Brussels, 28 April 2020 REGISTER OF FOOD ENZYMES TO BE CONSIDERED FOR INCLUSION IN THE UNION LIST Article 17 of Regulation (EC) No 1332/20081 provides for the establishment of a Register of all food enzymes to be considered for inclusion in the Union list. In accordance with that Article, the Register includes all applications which were submitted within the initial period fixed by that Regulation and which comply with the validity criteria laid down in accordance with Article 9(1) of (EC) No 1331/2008 establishing a common authorisation procedure for food additives, food enzymes and food flavourings2. The Register therefore lists all valid food enzyme applications submitted until 11 March 2015 except those withdrawn by the applicant before that date. Applications submitted after that date are not included in the Register but will be processed in accordance with the Common Authorisation Procedure. The entry of a food enzyme in the Register specifies the identification, the name, the source of the food enzyme as provided by the applicant and the EFSA question number under which the status of the Authority’s assessment can be followed3. As defined by Article 3 of Regulation (EC) No 1332/2008, ‘food enzyme’ subject to an entry in the Register, refers to a product that may contain more than one enzyme capable of catalysing a specific biochemical reaction. In the assessment process, such a food enzyme may be linked with several EFSA question numbers. -
Hypoxic-Induced Truncation of Voltage-Dependent Anion Channel 1 Is Mediated by Both Asparagine Endopeptidase and Calpain 1 Activities
www.impactjournals.com/oncotarget/ Oncotarget, 2018, Vol. 9, (No. 16), pp: 12825-12841 Research Paper Hypoxic-induced truncation of voltage-dependent anion channel 1 is mediated by both asparagine endopeptidase and calpain 1 activities Hadas Pahima1,*, Simona Reina2,3,*, Noa Tadmor1,*, Daniella Dadon-Klein1,*, Anna Shteinfer-Kuzmine1, Nathalie M. Mazure4,5, Vito De Pinto2 and Varda Shoshan- Barmatz1 1Department of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel 2Department of Biomedicine and Biotechnology, University of Catania and National Institute for Biomembranes and Biosystems, Section of Catania, Catania 95125, Italy 3Department of Biological, Geological and Environmental Sciences, University of Catania, Catania 95125, Italy 4Institute for Research on Cancer and Aging of Nice, University of Nice Sophia-Antipolis, Centre Antoine Lacassagne, Nice 06189, France 5Present address: INSERM U1065, C3M, Nice 06204, France *These authors contributed equally to this work Correspondence to: Varda Shoshan-Barmatz, email: [email protected] Keywords: asparagine endopeptidase; calpain; hypoxia; VDAC1 Abbreviations: AEP: asparagine endopeptidase; VDAC1: voltage-dependent anion channel 1 Received: October 09, 2017 Accepted: January 25, 2018 Published: January 31, 2018 Copyright: Pahima et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT The voltage-dependent anion channel 1 (VDAC1), an outer mitochondria membrane (OMM) protein, serves as a mitochondrial gatekeeper, mediating the transport of nucleotides, Ca2+ and other metabolites across the OMM.