Engineering the Residual Side Chains of HAP Phytases to Improve Their
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Phytic Acid (Phytate)/ Total Phosphorus
www.megazyme.com PHYTIC ACID (PHYTATE)/ TOTAL PHOSPHORUS Measured as phosphorus released by phytase and alkaline phosphatase ASSAY PROCEDURE K-PHYT 05/19 (50 Assays per Kit) © Megazyme 2019 INTRODUCTION: Phytic acid (phytate; myo-inositol 1,2,3,4,5,6-hexakisphosphate) is the primary source of inositol and storage phosphorus in plant seeds contributing ~ 70% of total phosphorus. The abundance of phytic acid in cereal grains is a concern in the foods and animal feeds industries because the phosphorus in this form is unavailable to monogastric animals due to a lack of endogenous phytases; enzymes specific for the dephosphorylation of phytic acid. In addition, the strong chelating characteristic of phytic acid reduces the bioavailability of other essential dietary nutrients such as minerals (e.g. Ca2+, Zn2+, Mg2+, Mn2+, Fe2+/3+), proteins and amino acids.2 High phytic acid content feeds are generally supplemented with inorganic phosphate, however this causes increased faecal phosphate levels and subsequent eutrophication of waterways. Alternatively, supplementation with commercial phytases is becoming increasingly popular and reduces the requirement for inorganic phosphate supplementation as well as the associated environmental issues. Currently, there is no commercially available, simple, quantitative method for phytic acid and, while such measurement is relatively complex, the generally accepted AOAC Method 986.11 has limitations.3 For each individual analysis the method requires cumbersome anion-exchange purification and a major inherent assumption here is that only phytic acid is purified. While this assumption is viable for non-processed grains for which phytic acid comprises at least 97% of total inositol phosphates, it is not viable for processed foods and feeds which can contain higher levels of some lower myo-inositol phosphate forms (i.e. -
Effect of Ph and Temperature on the Activity of Phytase Products Used In
Brazilian Journal of Poultry Science Revista Brasileira de Ciência Avícola Effect of ph and Temperature on the Activity of ISSN 1516-635X Jul - Sept 2012/ v.14 / n.3 / 159-232 Phytase Products Used in Broiler Nutrition Author(s) ABSTRACT Naves L de P1 Corrêa AD2 The activity of three commercial microbial phytase (Aspergillus Bertechini AG3 oryzae, A. niger, and Saccharomyces cerevisae) products used in broiler Gomide EM4 Santos CD dos2 nutrition was determined at different pH (2.0 to 9.0) and temperature (20 to 90°C) values. Enzymatic activity was determined according to the reaction of the phytase with its substrate (sodium phytate), in four replicates, and was expressed in units of phytase activity (FTU). A. oryzae phytase exhibited optimal activity at pH 4.0 and 40°C, but 1Graduate student in Monogastric Nutrition of its absolute activity was the lowest of the three phytases evaluated. the Animal Science Department − Federal A. niger phytase exhibited maximal activity close to pH 5.0 and 45oC, University of Lavras (UFLA). whereas S. cerevisae phytase presented its highest activity at pH close to 2Professor of the Chemistry Department/ UFLA. 4.5 and temperatures ranging between 50 and 60°C. It was concluded 3Professor of the Animal Science Department/ that A. niger and S. cerevisae phytase products exhibited the highest UFLA. absolute activities in vitro at pH and temperature values (pH lower than 4Ph. D. student in Monogastric Nutrition of o the Animal Science Department/UFLA. 5.0 and 41 C) corresponding to the ideal physiological conditions of broilers, which would theoretically allow high hydrolysis rate of the phytate contained in the feed. -
Peraturan Badan Pengawas Obat Dan Makanan Nomor 28 Tahun 2019 Tentang Bahan Penolong Dalam Pengolahan Pangan
BADAN PENGAWAS OBAT DAN MAKANAN REPUBLIK INDONESIA PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN NOMOR 28 TAHUN 2019 TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN DENGAN RAHMAT TUHAN YANG MAHA ESA KEPALA BADAN PENGAWAS OBAT DAN MAKANAN, Menimbang : a. bahwa masyarakat perlu dilindungi dari penggunaan bahan penolong yang tidak memenuhi persyaratan kesehatan; b. bahwa pengaturan terhadap Bahan Penolong dalam Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 10 Tahun 2016 tentang Penggunaan Bahan Penolong Golongan Enzim dan Golongan Penjerap Enzim dalam Pengolahan Pangan dan Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 7 Tahun 2015 tentang Penggunaan Amonium Sulfat sebagai Bahan Penolong dalam Proses Pengolahan Nata de Coco sudah tidak sesuai dengan kebutuhan hukum serta perkembangan ilmu pengetahuan dan teknologi sehingga perlu diganti; c. bahwa berdasarkan pertimbangan sebagaimana dimaksud dalam huruf a dan huruf b, perlu menetapkan Peraturan Badan Pengawas Obat dan Makanan tentang Bahan Penolong dalam Pengolahan Pangan; -2- Mengingat : 1. Undang-Undang Nomor 18 Tahun 2012 tentang Pangan (Lembaran Negara Republik Indonesia Tahun 2012 Nomor 227, Tambahan Lembaran Negara Republik Indonesia Nomor 5360); 2. Peraturan Pemerintah Nomor 28 Tahun 2004 tentang Keamanan, Mutu dan Gizi Pangan (Lembaran Negara Republik Indonesia Tahun 2004 Nomor 107, Tambahan Lembaran Negara Republik Indonesia Nomor 4424); 3. Peraturan Presiden Nomor 80 Tahun 2017 tentang Badan Pengawas Obat dan Makanan (Lembaran Negara Republik Indonesia Tahun 2017 Nomor 180); 4. Peraturan Badan Pengawas Obat dan Makanan Nomor 12 Tahun 2018 tentang Organisasi dan Tata Kerja Unit Pelaksana Teknis di Lingkungan Badan Pengawas Obat dan Makanan (Berita Negara Republik Indonesia Tahun 2018 Nomor 784); MEMUTUSKAN: Menetapkan : PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN. -
Final Dilution in Petri Plates with the Experiment, the Birds Were Weighed on Day-Of-Hatch and D 7, 10, Proper Culture Media, Tryptic Soy Agar (Biokar)
Symposium on Gut Health in Production of Food Animals November 10–12, 2014, St. Louis, Missouri Program and Abstracts www.GutHealthSymposium.com/2014 SYMPOSIUM ON GUT HEALTH IN PRODUCTION OF FOOD ANIMALS CONTENTS Welcome ............................................................................................................................3 Map ....................................................................................................................................4 Program .............................................................................................................................5 Poster Presentations......................................................................................................10 Abstracts .........................................................................................................................12 Poster Abstracts .............................................................................................................26 1 SYMPOSIUM ON GUT HEALTH IN PRODUCTION OF FOOD ANIMALS WELCOME On behalf of the Organizing Committee for the 3rd Symposium on Gut Health in Production of Food Animals, I welcome you to St. Louis, Missouri! I hope that the change in venue has made travel to the symposium easier and less expensive. Like the first two symposia organized around the topic of gut health in food animals, the aim this year is to bring together a group of scientists from academia, government, and industry to discuss the role of gut health in animal production and the essential -
<I>AUREOCOCCUS ANOPHAGEFFERENS</I>
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 12-2016 MOLECULAR AND ECOLOGICAL ASPECTS OF THE INTERACTIONS BETWEEN AUREOCOCCUS ANOPHAGEFFERENS AND ITS GIANT VIRUS Mohammad Moniruzzaman University of Tennessee, Knoxville, [email protected] Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Environmental Microbiology and Microbial Ecology Commons Recommended Citation Moniruzzaman, Mohammad, "MOLECULAR AND ECOLOGICAL ASPECTS OF THE INTERACTIONS BETWEEN AUREOCOCCUS ANOPHAGEFFERENS AND ITS GIANT VIRUS. " PhD diss., University of Tennessee, 2016. https://trace.tennessee.edu/utk_graddiss/4152 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Mohammad Moniruzzaman entitled "MOLECULAR AND ECOLOGICAL ASPECTS OF THE INTERACTIONS BETWEEN AUREOCOCCUS ANOPHAGEFFERENS AND ITS GIANT VIRUS." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Microbiology. Steven W. Wilhelm, Major Professor We have read this dissertation -
Solarbio Catalogue with PRICES
CAS Name Grade Purity Biochemical Reagent Biochemical Reagent 75621-03-3 C8390-1 3-((3-Cholamidopropyl)dimethylammonium)-1-propanesulfonateCHAPS Ultra Pure Grade 1g 75621-03-3 C8390-5 3-((3-Cholamidopropyl)dimethylammonium)-1-propanesulfonateCHAPS 5g 57-09-0 C8440-25 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 25g 57-09-0 C8440-100 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 100g 57-09-0 C8440-500 Cetyl-trimethyl Ammonium Bromide CTAB High Pure Grade ≥99.0% 500g E1170-100 0.5M EDTA (PH8.0) 100ml E1170-500 0.5M EDTA (PH8.0) 500ml 6381-92-6 E8030-100 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 100g 6381-92-6 E8030-500 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 500g 6381-92-6 E8030-1000 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 1kg 6381-92-6 E8030-5000 EDTA disodium salt dihydrate EDTA Na2 Biotechnology Grade ≥99.0% 5kg 60-00-4 E8040-100 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 100g 60-00-4 E8040-500 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 500g 60-00-4 E8040-1000 Ethylenediaminetetraacetic acid EDTA Ultra Pure Grade ≥99.5% 1kg 67-42-5 E8050-5 Ethylene glycol-bis(2-aminoethylether)-N,N,NEGTA′,N′-tetraacetic acid Ultra Pure Grade ≥97.0% 5g 67-42-5 E8050-10 Ethylene glycol-bis(2-aminoethylether)-N,N,NEGTA′,N′-tetraacetic acid Ultra Pure Grade ≥97.0% 10g 50-01-1 G8070-100 Guanidine Hydrochloride Guanidine HCl ≥98.0%(AT) 100g 50-01-1 G8070-500 Guanidine Hydrochloride Guanidine HCl ≥98.0%(AT) 500g 56-81-5 -
John H. Northrop
J OHN H . N ORTHROP T h e preparation of pure enzymes and virus proteins* Nobel Lecture, December 12, 1946 The problem of the chemical nature of the substances which control the reactions occurring in living cells has been a subject of research, and also of controversy, for nearly two hundred years. Before the eighteenth century these reactions were considered as "vital processes", outside the realm of experimental science. The work of Spallanzani, Payen and Persoz, Schwann, Kühne, and finally Buchner proved that many of these reactions could take place without living cells and were probably caused by the presence of small amounts of unstable and active substances, which Kühne called "enzymes". Berzelius, a century ago, pointed out that these enzymes were similar to the catalysts of the chemist and suggested that they be considered as special catalysts formed by the cells. This hypothesis was far ahead of its time and met with great opposition, since many workers considered that enzyme reac- tions differed qualitatively from ordinary chemical reactions. The work of Tamman, Arrhenius, Henri, Michaelis, Nelson, von Euler, Willstätter, War- burg, and other chemists, however, has shown that Berzelius’ viewpoint was correct and enzyme reactions are now considered a special kind of catalysis which does not differ qualitatively from other catalytic reactions. While the study of enzyme reactions made rapid progress all attempts to isolate an enzyme and so determine its chemical nature were unsuccessful until recently. The early workers were of the opinion that enzymes were probably pro- teins and in 1896 Pekelharing isolated a protein from gastric juice which he considered to be the enzyme pepsin. -
Phosphodiesterases
^ ^ ^ ^ I ^ ^ ^ ^ II ^ II ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ ^ I ^ � European Patent Office Office europeen des brevets EP 0 967 284 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) |nt CI* C12N 15/55, C12N 9/16, 29.12.1999 Bulletin 1999/52 qq-) N 33/68, C12Q 1/44, C07 K 1 6/40 C 1 2 N 1 5/1 1 v(21)to i ;\ Appa hcation, ♦■ number:k 99303985.8QQinioQc fi ,' ,' A61 K 38/46, A61 K 35/00, (22) Date of filing: 21.05.1999 A61 K 48/00 (84) Designated Contracting States: (72) Inventors: AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU • Lanfear, Jeremy, c/o Pfizer Central Research MC NL PT SE Sandwich, Kent CT13 9NJ (GB) Designated Extension States: • Robas, Nicola Melanie, AL LT LV MK RO SI c/o Pfizer Central Research Sandwich, Kent CT13 9NJ (GB) (30) Priority: 28.05.1998 GB 9811500 30.10.1998 GB 9823882 (74) Representative: Harding, Charles Thomas et al 04.12.1998 GB 9826777 D. Young & Co. 09.04.1999 GB 9908247 21 New Fetter Lane 10.05.1999 GB9910801 London EC4A 1 DA (GB) (83) Declaration under Rule 28(4) EPC (expert Remarks: solution) The applicant has subsequently filed a sequence listing and declared, that it includes no new matter. (71) Applicants: • Pfizer Limited Sandwich Kent CT13 9NJ (GB) Designated Contracting States: GB • PFIZER INC. Groton, CT 06340 (US) Designated Contracting States: BE CH DE DK ES FI FR GR IE IT LI LU MC PT SE AT CY (54) Phosphodiesterases (57) Amino acid sequences and nucleotide se- SEQ ID No. -
DUAL ROLE of CATHEPSIN D: LIGAND and PROTEASE Martin Fuseka, Václav Větvičkab
Biomed. Papers 149(1), 43–50 (2005) 43 © M. Fusek, V. Větvička DUAL ROLE OF CATHEPSIN D: LIGAND AND PROTEASE Martin Fuseka, Václav Větvičkab* a Institute of Organic Chemistry and Biochemistry, CAS, Prague, Czech Republic, and b University of Louisville, Department of Pathology, Louisville, KY40292, USA, e-mail: [email protected] Received: April 15, 2005; Accepted (with revisions): June 20, 2005 Key words: Cathepsin D/Procathepsin D/Cancer/Activation peptide/Mitogenic activity/Proliferation Cathepsin D is peptidase belonging to the family of aspartic peptidases. Its mostly described function is intracel- lular catabolism in lysosomal compartments, other physiological effect include hormone and antigen processing. For almost two decades, there have been an increasing number of data describing additional roles imparted by cathepsin D and its pro-enzyme, resulting in cathepsin D being a specific biomarker of some diseases. These roles in pathological conditions, namely elevated levels in certain tumor tissues, seem to be connected to another, yet not fully understood functionality. However, despite numerous studies, the mechanisms of cathepsin D and its precursor’s actions are still not completely understood. From results discussed in this article it might be concluded that cathepsin D in its zymogen status has additional function, which is rather dependent on a “ligand-like” function then on proteolytic activity. CATHEPSIN D – MEMBER PRIMARY, SECONDARY AND TERTIARY OF ASPARTIC PEPTIDASES FAMILY STRUCTURES OF ASPARTIC PEPTIDASES Major function of cathepsin D is the digestion of There is a high degree of sequence similarity among proteins and peptides within the acidic compartment eukaryotic members of the family of aspartic peptidases, of lysosome1. -
Hydrolysis of -Lactalbumin by Chymosin and Pepsin. Effect Of
Hydrolysis of α-lactalbumin by chymosin and pepsin. Effect of conformation and pH G. Miranda, G. Hazé, Non Renseigné To cite this version: G. Miranda, G. Hazé, Non Renseigné. Hydrolysis of α-lactalbumin by chymosin and pepsin. Effect of conformation and pH. Le Lait, INRA Editions, 1989, 69 (6), pp.451-459. hal-00929176 HAL Id: hal-00929176 https://hal.archives-ouvertes.fr/hal-00929176 Submitted on 1 Jan 1989 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. Lait (1989) 69. 451-459 451 © Elsevier/INRA Original article Hydrolysis of œ-lactalburnin by chymosin and pepsin. Effect of conformation and pH G. Miranda, G. Hazé, P.Scanff and J.P.Pélissier INRA, station de recherches laitières, 78350 Jouy-en-Josas, France (received 21 March 1989. accepted 26 June 1989) Summary - The correlation between change of conformation of a-Iactalbumin and its degradation by gastric enzymes was verified. With citrate buffer (0.1 M), the modification of a-Iactalbumin confor- mation occurred when the pH value was below pH 4.0. This conformational change was influenced by buffer composition and ionic strength. However, the presence of EDTA in the butter did not modi- fy the pH value at which the change of conformation of the protein occurred. -
2014 Annual Meeting Abstracts
Poultry Science Association 103rd Annual Meeting Abstracts To be presented July 14–17, 2014 Corpus Christi, Texas Also contains abstracts from the 2014 International Poultry Scientific Forum January 27–28, 2014 EDITOR-IN-CHIEF ® T. E. Porter (2016) POULTRY SCIENCE SECTION EDITORS ASSOCIATE EDITORS (2013–2014) Environment, Well-Being, N. Acar (2015) I. Hanning (2016) M. Pines (2014) and Behavior O. Adeola (2015) W. Huff (2014) T. Poole (2016) I. Estevez (2014) H. Ahmadi (2013) R. M. Hulet (2014) R. Poureslami (2015) M. M. Beck (2016) W. Alali (2016) M. Hume (2015) A. Pradhan (2014) T. J. Applegate (2015) A. Jackson-Davis (2016) G.-H. Qi (2015) Genetics C. Ashwell (2016) D. Jackwood (2014) G. Rajashekara (2014) J. Dodgson (2016) D. Babu (2015) P. A. Johnson (2016) V. Ravindran (2015) Immunology, Health, K. Bafundo (2016) C. Jones (2016) K. Reed (2016) and Disease M. R. Bakst (2014) P. Kaiser (2014) T. B. Rodenburg (2014) R. L. Taylor Jr. (2016) R. Beckstead (2016) I. Kang (2015) G. J. M. Rosa (2016) B. R. Behrends (2016) N. Kansaku (2016) W. B. Roush (2013) Metabolism and Nutrition L. Berghman (2014) E. Kebreab (2013) I. Rozenboim (2014) G. Cherian (2014) W. Berry (2014) E. J. Kim (2016) C. Ruiz-Feria (2013) M. Rodehutscord (2016) D. Biswas (2014) W. Kim (2016) S. M. Rutherfurd (2015) E. Esteve-Garcia (2014) J. Brake (2013) M. Koci (2015) M. Schilling (2015) K. Bregendahl (2014) K. W. Koelkebeck (2013) C. Schmidt (2016) Molecular, Cellular, B. Brehm-Stecher (2016) M. H. Kogut (2014) P. Selle (2013) and Developmental Biology J. -
Structure of the Human Renin Gene
Proc. Nati. Acad. Sci. USA Vol. 81, pp. 5999-6003, October 1984 Biochemistry Structure of the human renin gene (hypertension/aspartyl proteinase/nucleotide sequence/splice junction) HITOSHI MIYAZAKI*, AKIYOSHI FUKAMIZU*, SHIGEHISA HIROSE*, TAKASHI HAYASHI*, HITOSHI HORI*, HIROAKI OHKUBOt, SHIGETADA NAKANISHIt, AND KAZUO MURAKAMI** *Institute of Applied Biochemistry, University of Tsukuba, Ibaraki 305, Japan; and tInstitute for Immunology, Kyoto University Faculty of Medicine, Kyoto 606, Japan Communicated by Leroy Hood, June 27, 1984 ABSTRACT The human renin gene was isolated from a between the intron-exon organization of the gene and the Charon 4A human genomic library and characterized. The tertiary structure of the protein. gene spans about 11.7 kilobases and consists of 10 exons and 9 introns that map at points that could be variable surface loops MATERIALS AND METHODS of the enzyme. The complete coding regions, the 5'- and 3'- Materials. All restriction enzymes were obtained from flanking regions, and the exon-intron boundaries were se- either New England Biolabs or Takara Shuzo (Kyoto, Ja- quenced. The active site aspartyl residues Asp-38 and Asp-226 pan). Escherichia coli alkaline phosphatase and T4 DNA li- are encoded by the third and eighth exons, respectively. The gase were from Takara Shuzo. [_y-32P]ATP (>5000 Ci/mmol; extra three amino acids (Asp-165, Ser-166, Glu-167) that are 1 Ci = 37 GBq) and [a-32P]dCTP (=3000 Ci/mmol) were not present in mouse renin are encoded by the separate sixth from Amersham. exon, an exon as small as 9 nucleotides. The positions of the Screening. A human genomic library, prepared from partial introns are in remarkable agreement with those in the human Alu I and Hae III digestion and ligated into the EcoRI arms pepsin gene, supporting the view that the genes coding for of the X vector Charon 4A, was kindly provided by T.