Guidelines for Meat Color Evaluation
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Colors and Fillstyle
GraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphicsGraphics andandandandandandandandandandandandandandandandandandandandandandandandandandandandandand TTTTTTTTTTTTTTTTTTETETETETETXETXETXETXETXETXETXETXEXEXEXEXEXEXEXEXEXEXEXEXEXEXEXEXEXEXXXXX Ordinary colors More colors Colorful Fill—in style Custom colors From one color to another Tricks Online L Part II – Graphics AT EX Tutorial PSTricks c 2002, 2003, The Indian T This document is generated by hyperref, pstricks, pdftricks and pdfscreen packages on an intel and is released under EX Users Group The Indian T pc pdf running Floor lppl T Trivandrum 695014, EX with iii, sjp http://www.tug.org.in gnu/linux Buildings,EX Users Cotton HillsGroup india 1/19 Ordinary colors More colors Fill—in style Custom colors From one color to another 2. Colorful Tricks Seeing the (ps)tricks so far, at least some of you may be wishing for a bit of color in the graphics. Here’s good news for such people: you can have your wish! PSTricks comes with a set of macros that provide a basic set of colors Online LAT X Tutorial and lets you define your own colors. However, it has some incompatibility with E the LATEX package color. However, David Carlisle has written a package pstcol Part II – Graphics which modifies the PSTricks color interface to work with LATEX colors. All of our examples in this chapter assumes that this package is loaded, using the PSTricks command \usepackage{pstcol} in the preamble. Note that this loads the pstricks package also, so that it need not be separately loaded. c 2002, 2003, The Indian TEX Users Group This document is generated by pdfTEX with hyperref, pstricks, pdftricks and pdfscreen packages on an intel pc running gnu/linux and is released under lppl The Indian TEX Users Group Floor iii, sjp Buildings, Cotton Hills Trivandrum 695014, india http://www.tug.org.in 2/19 Colorful Tricks 2.1. -
Review of Measures for Light-Source Color Rendition and Considerations for a Two-Measure System for Characterizing Color Rendition
Review of measures for light-source color rendition and considerations for a two-measure system for characterizing color rendition Kevin W. Houser,1,* Minchen Wei,1 Aurélien David,2 Michael R. Krames,2 and Xiangyou Sharon Shen3 1Department of Architectural Engineering, The Pennsylvania State University, University Park, PA, 16802, USA 2Soraa, Inc., Fremont, CA 94555, USA 3Inno-Solution Research LLC, 913 Ringneck Road, State College, PA 16801, USA *[email protected] Abstract: Twenty-two measures of color rendition have been reviewed and summarized. Each measure was computed for 401 illuminants comprising incandescent, light-emitting diode (LED) -phosphor, LED-mixed, fluorescent, high-intensity discharge (HID), and theoretical illuminants. A multidimensional scaling analysis (Matrix Stress = 0.0731, R2 = 0.976) illustrates that the 22 measures cluster into three neighborhoods in a two- dimensional space, where the dimensions relate to color discrimination and color preference. When just two measures are used to characterize overall color rendition, the most information can be conveyed if one is a reference- based measure that is consistent with the concept of color fidelity or quality (e.g., Qa) and the other is a measure of relative gamut (e.g., Qg). ©2013 Optical Society of America OCIS codes: (330.1690) Color; (330.1715) Color, rendering and metamerism; (230.3670) Light-emitting diodes. References and links 1. CIE, “Methods of measuring and specifying colour rendering properties of light sources,” in CIE 13 (CIE, Vienna, Austria, 1965). 2. W. Walter, “How meaningful is the CIE color rendering index?” Light Design Appl. 11(2), 13–15 (1981). 3. T. Seim, “In search of an improved method for assessing the colour rendering properties of light sources,” Lighting Res. -
Color Measurement1 Agr1c Ü8 ,
I A^w /\PK4 1946 USDA COLOR MEASUREMENT1 AGR1C ü8 , ,. 2001 DEC-1 f=> 7=50 AndA ItsT ApplicationA rL '"NT SERIAL Í to the Grading of Agricultural Products A HANDBOOK ON THE METHOD OF DISK COLORIMETRY ui By S3 DOROTHY NICKERSON, Color Technologist, Producdon and Marketing Administration 50! es tt^iSi as U. S. DEPARTMENT OF AGRICULTURE Miscellaneous Publication 580 March 1946 CONTENTS Page Introduction 1 Color-grading problems 1 Color charts in grading work 2 Transparent-color standards in grading work 3 Standards need measuring 4 Several methods of expressing results of color measurement 5 I.C.I, method of color notation 6 Homogeneous-heterogeneous method of color notation 6 Munsell method of color notation 7 Relation between methods 9 Disk colorimetry 10 Early method 22 Present method 22 Instruments 23 Choice of disks 25 Conversion to Munsell notation 37 Application of disk colorimetry to grading problems 38 Sample preparation 38 Preparation of conversion data 40 Applications of Munsell notations in related problems 45 The Kelly mask method for color matching 47 Standard names for colors 48 A.S.A. standard for the specification and description of color 50 Color-tolerance specifications 52 Artificial daylighting for grading work 53 Color-vision testing 59 Literature cited 61 666177—46- COLOR MEASUREMENT And Its Application to the Grading of Agricultural Products By DOROTHY NICKERSON, color technologist Production and Marketing Administration INTRODUCTION cotton, hay, butter, cheese, eggs, fruits and vegetables (fresh, canned, frozen, and dried), honey, tobacco, In the 16 years since publication of the disk method 3 1 cereal grains, meats, and rosin. -
Strategies for Increasing Oxidative Stability of (Fresh) Meat Color
O X I D A T I V E P R O C E S S E S I N M E A T Strategies for Increasing Oxidative Stability of (Fresh) Meat Color CAMERON FAUSTMAN*, W.K.M. CHAN, M.P. LYNCH and S.T. JOO Introduction moglobin and myoglobin) and for electron transport during respiration (cytochromes) in the living animal. Skeletal Fresh meat color is determined by the oxidation status muscles which obtain energy primarily by aerobic means of myoglobin. Several reviews of myoglobin chemistry and contain relatively high concentrations of heme proteins when meat color stability, including cured and/or cooked meat compared to those which depend primarily on anaerobic color, have been published (Livingston and Brown, 1981; glycolysis. Giddings, 1977; Faustman and Cassens, 1990a; Renerre, Of the heme proteins found in post-mortem skeletal 1990; Cornforth, 1994). The purpose of this presentation is muscle, myoglobin is the most important for considerations to emphasize recent research findings which impact the oxi- of meat color. The majority of hemoglobin found in the liv- dative stability of myoglobin in fresh meat. Specific atten- ing animal is lost during slaughter as a result of exsan- tion is given to metmyoglobin reduction and antioxidant ap- guination. Some blood is retained in meat (Fleming et al., proaches for minimizing oxymyoglobin oxidation. 1960) and Warriss and Rhodes (1977) estimated the aver- Maintenance of oxymyoglobin and thus a desirable age residual blood content of butcher’s meat to be 0.3%. appearance in fresh meat has significant economic impact. Han et al. (1994) recently published a procedure for deter- Liu et al. -
Relationship Between Beef Colour and Myoglobin
Relationship between beef colour and myoglobin Author: S.H.J.M . Dobbelstein Registration number: 790608185120 Subject code: P052-754 (24 stp) P052-274 (1 stp) Supervisors: Dr. Ir. E.U. Thoden van Velzen (A&F) Dr. Ir.J.P.H . Linssen (WUR) Examiner: Prof. Dr. Ir. M.A.J.S. van Boekel Report 474 Preface This thesis is part of my Master in Food Technology at Wageningen UR. This subject was carried out at the Quality in Chains department of Agrotechnology & Food Innovations (A&F) in co opération with the Product Design and Quality Management Group of Wageningen UR. I worked on this thesis from January till August 2005 at A&F. During my study I became interested in Meat Science and the subject of this thesis fits perfecdy to my interests. During my stay at A&F I had all freedom and responsibility to conduct my research. This made I really enjoyed working on this thesis. Moreover, it increased my knowledge of Meat Science very much. I would like to thank Ulphard Thoden van Velzen, my supervisor at A&F, and Jozef Linssen, my supervisor at the University, for their help during this study. I also want to thank Ronald Holtmaat from ProMessa (Deventer, NL) who kindly provided the meat for this study. Furthermore I would like to thank Aart Zegveld, Dianne Somhorst and Janny Slotboom who helped me with my practical work at A&F. ©Agrotechnology &Foo d Innovations B.V .Membe r of Wageningen UR Abstract The most important quality attribute of fresh beef is its colour. -
Relationship of Solid Ink Density and Dot Gain in Digital Printing
International Journal of Engineering and Technical Research (IJETR) ISSN: 2321-0869, Volume-2, Issue-7, July 2014 Relationship of Solid Ink Density and Dot Gain in Digital Printing Vikas Jangra, Abhishek Saini, Anil Kundu gain while meeting density requirements. As discussed Abstract— Ours is the generation which is living in the age of above Dot gain is the measurement of the increase in tone science and technology. The latest scientific inventions have value from original file to the printed sheet. given rise to various technologies in every aspect of our life. Newer technologies have entered the field of printing also. II. MATERIALS AND METHODS Digital printing is one of these latest technologies which have further revolutionized entire modern printing industry in many Densitometer is used for measuring density of ink ways. It also facilitates working on large variety of surfaces, on the paper. Densitometer can be classified according to besides these factors digital printing have grown widely and type of materials they are designed to measure i.e. opaque made a special impact in print market. The presented analysis and transparent. Density of opaque materials is measured by system is used for study of print quality in Digital Printing. reflected light with a device called reflection type densitometer. Density of transparent materials is measured Index Terms— Digital Printing, Dot Gain, Solid ink density, by transmitted light with a device called transmission type Coated Paper and Uncoated Paper. densitometer. In order to measure the print quality i.e. solid ink density (SID) and dot gain (DG) on coated and uncoated I. -
Myoglobin from Equine Skeletal Muscle
Myoglobin from equine skeletal muscle Catalog Number M0630 Storage Temperature –20 C CAS RN 100684-32-0 Precautions and Disclaimer This product is for R&D use only, not for drug, Product Description household, or other uses. Please consult the Safety Molecular mass:1 17.6 kDa Data Sheet for information regarding hazards and safe Extinction coefficient:2 EmM = 12.92 (555 nm) handling practices. pI:3 7.3 (major component) and 6.8 (minor component) Preparation Instructions Myoglobin from horse skeletal muscle is a single chain This protein is soluble in water (10 mg/ml), yielding a heme protein containing 153 amino acid residues. It clear, red brown solution. posesses no disulfide bridges or free -SH groups. Myoglobin contains 8 variously sized right-handed References helical regions, joined by non-ordered or random coil 1. Darbre, P.D. et al., Comparison of the myoglobin of regions. These 8 helices (A, B, C, D, E, F, G, and H) the zebra (Equus burchelli) with that of the horse are folded back on top of one another, and the heme is (Equus cabalus). Biochim. Biophys. Acta, 393(1), situated between helices E and F. The heme is almost 201-204 (1975). totally buried. Only the edge carrying the two 2. Bowen, W.J., The absorption spectra and extinction hydrophylic propionic acid groups is exposed. The coefficients of myoglobin. J. Biol. Chem., 179, 235- heme is held in position by a coordinating complex 245 (1949). between the central Fe(II) atom and 2 histidine residues 3. Radola, B.J., Isoelectric focusing in layers of (on helices E and F, respectively). -
1 Hemoglobin Catalyzes ATP-Synthesis in Human
Hemoglobin catalyzes ATP-synthesis in human erythrocytes: A murburn model Abhinav Parashar*, Vivian David Jacob, Daniel Andrew Gideon, Kelath Murali Manoj* *Corresponding authors, Satyamjayatu: The Science & Ethics Foundation, Snehatheeram, Kulappully, Shoranur-2, Kerala, India-679122. [email protected] Abstract: Blood hemoglobin (Hb) is the most abundant globular protein in humans, known to transport oxygen. Erythrocytes have ~10-3 M concentration levels of ATP in steady-state and we estimate that this high cannot be formed from 10-4 - 10-7 M levels of precursors via substrate- level phosphorylation of glycolysis. To account for this discrepancy, we propose that Hb serves as a ‘murzyme’ (a redox enzyme working along the principles of murburn concept), catalyzing the synthesis of the major amounts of ATP found in erythrocytes. This proposal is along the lines of our earlier works demonstrating DROS (diffusible reactive oxygen species) mediated ATP- synthesis as a thermodynamically and kinetically viable mechanism for physiological oxidative phosphorylation. We support the new hypothesis for Hb with theoretical arguments, experimental findings of reputed peers and in silico explorations. Using in silico methods, we demonstrate that adenoside nucleotide and 2,3-bisphosphoglycerate (2,3-BPG) binding sites are located suitably on the monomer/tetramer, thereby availing facile access to the superoxide emanating from the heme center. Our proposal explains earlier reported in situ experimental findings/suggestions of 2,3-BPG and ADP binding at the same locus on Hb. The binding energy is in the order of 2,3-BPG > NADH > ATP > ADP > AMP and agrees with earlier reports, potentially explaining the bioenergetic physiology of erythrocytes. -
Chromatic Adaptation Transform by Spectral Reconstruction Scott A
Chromatic Adaptation Transform by Spectral Reconstruction Scott A. Burns, University of Illinois at Urbana-Champaign, [email protected] February 28, 2019 Note to readers: This version of the paper is a preprint of a paper to appear in Color Research and Application in October 2019 (Citation: Burns SA. Chromatic adaptation transform by spectral reconstruction. Color Res Appl. 2019;44(5):682-693). The full text of the final version is available courtesy of Wiley Content Sharing initiative at: https://rdcu.be/bEZbD. The final published version differs substantially from the preprint shown here, as follows. The claims of negative tristimulus values being “failures” of a CAT are removed, since in some circumstances such as with “supersaturated” colors, it may be reasonable for a CAT to produce such results. The revised version simply states that in certain applications, tristimulus values outside the spectral locus or having negative values are undesirable. In these cases, the proposed method will guarantee that the destination colors will always be within the spectral locus. Abstract: A color appearance model (CAM) is an advanced colorimetric tool used to predict color appearance under a wide variety of viewing conditions. A chromatic adaptation transform (CAT) is an integral part of a CAM. Its role is to predict “corresponding colors,” that is, a pair of colors that have the same color appearance when viewed under different illuminants, after partial or full adaptation to each illuminant. Modern CATs perform well when applied to a limited range of illuminant pairs and a limited range of source (test) colors. However, they can fail if operated outside these ranges. -
As Well As Whale Metmyoglobin in 0.1 M Deuterated Phosphate at Pd 7 and at 31'C
NUCLEAR MAGNETIC RESONANCE STUDIES OF HEMOGLOBINS, III. EVIDENCE 1OR THE NONEQUIVALENCE OF a- AND (3-CHAINS IN AZIDE DERIVATIVES OF AME'TIIEMOGLOBINS* BY DONALD G. DAVIS, SAMUEL CHARACIHEt AND) CHIEN Ho DEPARTMENT OF BIOPHYSICS AND MICRtOBIOLOGY, UNJVI;RSI'IY' OlF Pl-ITT'SlBURGH, PITTSBURGH, PENNSYLVANIA Communicated by George Scatchard, June 12, 1969 Abstract.-Nuclear magnetic resonance spectroscopy (100-MN1Hz proton) was used to study the low-spin (S = 1/2) azide derivatives of human adult (a2(32), human fetal (C2Y2), Zurich (a2,f263 HiS - Arg), and horse (a2'(32') methemoglobins, as well as whale metmyoglobin in 0.1 M deuterated phosphate at pD 7 and at 31'C. The experimental results indicate that the azide-bound heme groups of the a- and (-chains in human adult methemoglobin and of the a- and 'y-chains in fetal methemoglobin are not equivalent. The affinity of the (3- or e-chain for azide ion appears larger than that of the a-chain. The nuclar magnetic resonance spectrum of hemoglobin Zfirich shows that the environment of the azide-heme complex in the abnormal (-chain is altered by the substitution of arginine for histidine in the (3-63 position, while the a-heme environment remains unaffected. Introduction.-The chief physiologic function of hemoglobin is to transport molecular oxygen from lung to tissues by virtue of its ability to combine revers- ibly with oxygen. Hemoglobin is a protein molecule consisting of four subunits (normally two a-chains and two (3-chains). Each of the four subunits has a heme group, and these heme groups are the "active centers" of hemoglobin. -
ARC Laboratory Handbook. Vol. 5 Colour: Specification and Measurement
Andrea Urland CONSERVATION OF ARCHITECTURAL HERITAGE, OFARCHITECTURALHERITAGE, CONSERVATION Colour Specification andmeasurement HISTORIC STRUCTURESANDMATERIALS UNESCO ICCROM WHC VOLUME ARC 5 /99 LABORATCOROY HLANODBOUOKR The ICCROM ARC Laboratory Handbook is intended to assist professionals working in the field of conserva- tion of architectural heritage and historic structures. It has been prepared mainly for architects and engineers, but may also be relevant for conservator-restorers or archaeologists. It aims to: - offer an overview of each problem area combined with laboratory practicals and case studies; - describe some of the most widely used practices and illustrate the various approaches to the analysis of materials and their deterioration; - facilitate interdisciplinary teamwork among scientists and other professionals involved in the conservation process. The Handbook has evolved from lecture and laboratory handouts that have been developed for the ICCROM training programmes. It has been devised within the framework of the current courses, principally the International Refresher Course on Conservation of Architectural Heritage and Historic Structures (ARC). The general layout of each volume is as follows: introductory information, explanations of scientific termi- nology, the most common problems met, types of analysis, laboratory tests, case studies and bibliography. The concept behind the Handbook is modular and it has been purposely structured as a series of independent volumes to allow: - authors to periodically update the -
AMSA Meat Color Measurement Guidelines
AMSA Meat Color Measurement Guidelines Revised December 2012 American Meat Science Association http://www.meatscience.org AMSA Meat Color Measurement Guidelines Revised December 2012 American Meat Science Association 201 West Springfield Avenue, Suite 1202 Champaign, Illinois USA 61820 800-517-2672 [email protected] http://www.meatscience.org CONTENTS Technical Writing Committee .................................................................................................................... v Preface ..............................................................................................................................................................vi Section I: Introduction ................................................................................................................................. 1 Section II: Myoglobin Chemistry ............................................................................................................... 3 A. Fundamental Myoglobin Chemistry ................................................................................................................ 3 B. Dynamics of Myoglobin Redox Form Interconversions ........................................................................... 3 C. Visual, Practical Meat Color Versus Actual Pigment Chemistry ........................................................... 5 D. Factors Affecting Meat Color ............................................................................................................................... 6 E. Muscle