DOCSLIB.ORG

Effect of Carbon Sources on Formation of Α-Amylase And

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Effect of Carbon Sources on Formation of Α-Amylase And J. Gen. App!. Microbiol,, 21, 51-59 (1975) EFFECT OF CARBON SOURCES ON FORMATION OF a-AMYLASE AND GLUCOAMYLASE BY CLOSTRIDIUM ACETOBUTYLICUM BURT ENSLEY, JOHN J. McHUGH, AND LARRY L. BARTON Department of Biology, University of New Mexico, Albuquerque, New Mexico 87131, U. S. A. (Received November 2, 1974) As determined by enzyme levels and by differential rate of enzyme formation, the synthesis of a-amylase and glucoamylase by Clostridium acetobutylicum is under separate regulatory systems. Induction of a- amylase occurs when starch is the carbon source while induction of glucoamylase accompanies growth with glucose. Minimal production of both enzymes is associated with growth on fructose, and intermediate levels result from growth with maltose. While both a-amylase and glucoamylase are elaborated into the culture fluid during the logarithmic growth phase, 41-44% of total amylase and 22-33 % of total glucoamylase remain associated with the bacterial cells. Studies involving cell fra- ctionation, cell washing, and pH-dependent adsorptions indicate that cell- associated a-amylase and glucoamylase are localized primarily with the surface of the cells and only to a small extent with the intracellular region. Many bacteria produce starch-hydrolyzing enzymes (1). Saccharification is usually attributed to a-amylase; however, a few bacteria are reported to have other types of starch-degrading enzymes. Pseudomonas stutzeri does not form an a- amylase but produces an enzyme which converts starch to maltotetrose (2) while Streptococcus equinus produces both a-amylase and a starch-hydrolyzing transgly- cosylase (3). Clostridium acetobutylicum hydrolyzes starch by two types of a- mylase (4). One is a-amylase [a-D-(l, 4)-glucan glucanohydrolase, EC 3.2.1.1] which converts starch to maltose and low molecular weight dextrins. The other is glucoamylase [a-D-(l, 4)-glucan glucohydrolase, EC 3.2.1.3], originally referred to as a maltase by HoCKENHULLand HERBERT(5), which splits starch to glucose by hydrolyzing both a-D-(1--4) and a-D-(l->6) glucosidic linkages. Index Words : a-amylase, formation by C. acetobutylicum; glucoamylase, formation by C. acetobutylicum; Clostridium acetobutylicum, amylases of. 51 52 ENSLEY, MCHUGH, and BARTON VOL. 21 The partially purified a-amylase from C. acetobutylicum has been reported to have a broad pH optimum curve with a midpoint at pH 4.8 and to hydrolyze starch, dextrin, and glycogen (5). The glucoamylase from C. acetobutylicum has not been purified but has been reported to release glucose from the non-reducing end of a starch chain. The rate of hydrolytic attack by glucoamylase is similar for maltose, amyloheptose, starch, and limit dextrin (6). Additionally, this glucoamylase is stable for several weeks at 37°, catalyzes quantitative hydrolysis of maltose to glucose, and has a pH optimum of 4.63 (5). Although the metabolism and physiology of C. acetobutylicum has been ex- tensively studied (7), the formation of starch-hydrolyzing enzymes has not been examined. This paper describes the formation of a-amylase and glucoamylase by C. acetobutylicum as influenced by the carbon source. MATERIALSAND METHODS Organism and media. C. acetobutylicum NRRL B 592, obtained from C. E. Georgi at the University of Nebraska, was maintained by periodic transfers in fluid thioglycolate medium (BBL). Media used to evaluate amylase production contained 0.8 % yeast extract (Difco), 0.05 % sodium thioglycolate (Difco), and 0.5 % glucose, maltose, fructose, or starch. When starch was the carbon source, 0.01 % glucose was added along with 0.49 % starch to decrease the length of the lag phase. Growth of organism for enzyme production. Media, 100 ml, were sterilized in 300 ml side-arm culture flasks fitted with serum stoppers. The flasks were thoroughly flushed with sterile nitrogen gas before being inoculated with 2 ml of a 6-hr culture grown in fluid thioglycolate. Incubation of the stationary culture was at 37°. At specific intervals, 4-ml samples were withdrawn from the culture and centrifuged at 8,000><9 for 20 min. The resulting centrifugate was used for enzyme measurements. Growth was determined by measuring the absorbance of the culture at 540 nm using a Bausch and Lomb Spectronic 20. The application of a slight negative pressure to the spectrophotometer tube enabled recording of cell densities without interference from gas bubbles. Increase in optical density of the culture was directly proportional to an increase in cellular dry weight. Glucoamylase measurements. The assay for glucoamylase was based on the quantity of glucose liberated from starch by enzymic hydrolysis. The culture fluid, 0.25 ml, was added to an equal volume of 2 % starch (Difco) in 0.1 M sodium acetate buffer, pH 4.5. Following aerobic incubation at 37° for 2 hr, the gluco- amylase activity was destroyed by placing the reaction tubes in boiling water for 2 min. Glucose liberated was quantitated by the colorometric glucose oxidase- peroxidase system previously described (8). A unit of glucoamylase was defined as the quantity of enzyme which liberated 1pmol of glucose per minute from 1975 Formation of Amylases by C. acetobutylicum 53 starch under the described conditions. a-Amylase measurements. Assays for a-amylase was based on the quantitation of reducing sugars resulting from enzymic hydrolysis of starch. The culture fluid, 1 ml, was mixed with an equal volume of 1 % starch (Difco) in 0.1 M sodium acetate, pH 4.6, which also contains 0.02 M CaC12. Incubation was at 37° for 20 min. Reducing sugars were measured using the 3, 5-dinitrosalicyclic acid reagent as described by WELKERand CAMPBELL(9) and calculated, in umol, from a standard curve previously calibrated against maltose. One unit of a-amylase activity was defined as the amount of enzyme releasing 1 pmol of reducing sugar per minute under the reaction conditions defined. Differential rate of enzyme formation. The growth rate is expressed as k, where k=A/t and A is the absorbance of the culture and t is the time of incubation in minutes. The values for determining k were taken from the growth curve cor- responding to the logarithmic phase. The expression of the rate of a-amylase and glucoamylase synthesis with respect to rate of growth is referred to as the dif- ferential rate of enzyme formation. The method for calculation of differential rate of enzyme synthesis follows previously established methods (9). The dif- ferential rate of a-amylase synthesis is referred to as Ka, where Ka= units of a- amylase/A. Similarly the differential rate of glucoamylase formation is expressed as Kg, where Kg= units of glucoamylase/A. Cellfree extracts. Following incubation periods of 4 and 10 hr, C. aceto- butylicum was removed from 200 ml of the glucose medium by centrifugation and washed twice with 0.01 N acetate buffer, pH 4.6. The cells were suspended in 20 ml of 0.01 N acetate buffer, pH 4.6, and disrupted by a single passage through a French pressure cell at 10,000 lb/in2 moval of cell debris was accomplished by centrifuga- tion at 8,000 x g for 20 min. Enzyme adsorption study. From a 4-hr culture growing in the glucose medium, 50 ml was withdrawn and divided into 10 ml fractions and adjusted to the desired pH with 0.02 N NaOH. Following incubation at room temperature for 15 min, the cells were removed by centrifugation and the centrifugate was dialyzed for 24 hr against 0.001 M sodium acetate, pH 4.6. The dialysate was assayed for both gluco- amylase and a-amylase. RESULTS a-Amylase and glucoamylase formation accompanying growth Both a-amylase and glucoamylase are produced by C. acetobutylicum during the logarithmic growth phase (Fig. 1). With glucoamylase, production occurs in the early portion of the logarithmic phase with maximum amount formed by the time the culture reaches the middle of this exponential growth period. On the other hand, elaboration of a-am lyase into the extracellular medium appears constant throughout the logarithmic growth phase. Metabolic activity of the culture is 54 ENSLEY, MCHUGH, and BARTON VOL. 21 Fig. 1. Characteristics of growth of C. acetobutylicum with glucose as a carbon source, including formation of glucoamylase and a-amylase. • Concentration of glucose in the medium, 0 absorbance of culture, extracellular glucoamylase, o extracellular a-amylase, and x pH of medium. very high during the time of formation of the amylases as evidenced by the rapid disappearance of glucose and corresponding production of organic acids. Spore formation, as determined by microscopic examination, did not occur until after 12 hr of incubation; therefore, neither formation nor liberation of the starch- hydrolyzing enzymes is attributed to sporulation. The type of carbohydrate used to support the growth of C. acetobutylicum greatly affects the quantity and time of synthesis of a-amylase and glycoamylase (Fig. 2). With glucoamylase, two patterns of enzyme formation are apparent. Early synthesis of glucoamylase leading to high levels of enzyme occurs with growth on glucose and maltose, while latter formation resulting in markedly lower levels of enzyme results with fructose and starch. With a-amylase, greatest levels of enzyme occurred with growth on starch, while an intermediate level resulted with glucose, and lowest levels resulted when growth was on maltose and fructose. None of the four carbohydrates tested pro- duced maximum levels of both enzymes; however, both enzymes are produced in appreciable levels. Lowest levels of both amylases are found with growth on fructose. The amount of growth resulting from the utilization of the carbohydrates does not effect formation of the amylases since glucose, maltose, and fructose have comparable levels of growth but different rates and amounts of enzyme formed. Growth is slowest with starch but resulted in the production of greatest levels of a-amylase.
Load more

Recommended publications
  • The Distribution of Carbohydrase Activities in the Small Intestine in Early Weaned Calves
    The Distribution of Carbohydrase Activities in the Small Intestine in Early Weaned Calves Toshikazu MIYASHIGEand Shigefusa YAHATA Chugoku National Agricultural Experiment Station, Oda-shi 694-01 (Received December 8, 1980) Abstract 1. The carbohydrase activities of the small intestine of early weaned calves were compared with those of nursing ones at 26 weeks of age. 2. In the early weaned calves, the pH value of content of the caecum was observed to be lower than that of the nursing ones, suggesting that more soluble carbohydrates would have escaped from ruminal fermentation and reached the caecum. 3. The values of maltase and iso maltase activities of the early weaned calves were not different from those of the nursing ones. However, maltase activity of the early weaned calves distributed more constantly with relatively high level all over the small intestine. Lactase activity of the early weaned calves was almost the same as that of the nursing ones. Dextranase and amylase activities were also found in the small intestine of the early weaned calves. Jpn. J. Zootech. Sci., 52 (7): 532-536, 1981 In the previous study1) with nursing calves, it was shown that intestinal maltase activity was very low and did not increase with age. But the pattern of the distri- bution of maltase activity in the small intestine apparently changed with age and higher activity of maltase was found in the lower part of the small intestine at 26 weeks of age. Although the meaning of this change is not known, it is supposed that the change of the pattern would be correlated with the increase of solid food intake.
    [Show full text]
  • Effect of a Multi-Carbohydrase and Phytase Complex on the Ileal And
    animals Article Effect of a Multi-Carbohydrase and Phytase Complex on the Ileal and Total Tract Digestibility of Nutrients in Cannulated Growing Pigs 1, 2, 1, 1 1 3 Jia-Cheng Yang y, Li Wang y, Ya-Kuan Huang y, Lei Zhang , Rui Ma , Si Gao , Chang-Min Hu 4, Jlali Maamer 5, Cozannet Pierre 5, Aurélie Preynat 5, Xin Gen Lei 6 and Lv-Hui Sun 1,* 1 Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; [email protected] (J.-C.Y.); [email protected] (Y.-K.H.); [email protected] (L.Z.); [email protected] (R.M.) 2 Institute of Animal Science, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China; [email protected] 3 Demonstration Center of Hubei Province for Experimental Animal Science Education, Huazhong Agricultural University, Wuhan 430070, China; [email protected] 4 College of Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China; [email protected] 5 Adisseo France S.A.S., Center of Expertise in Research and Nutrition, 03600 Commentry, France; [email protected] (J.M.); [email protected] (C.P.); [email protected] (A.P.) 6 Department of Animal Science, Cornell University, Ithaca, NY 14853, USA; [email protected] * Correspondence: [email protected]; Tel.: +86-130-0712-1983 These authors contributed equally to this work. y Received: 6 July 2020; Accepted: 14 August 2020; Published: 17 August 2020 Simple Summary: It is well accepted that monogastric livestock lack phytase in their gastrointestinal tracts.
    [Show full text]
  • Exogenous Enzymes As Zootechnical Additives in Animal Feed: a Review
    catalysts Review Exogenous Enzymes as Zootechnical Additives in Animal Feed: A Review Brianda Susana Velázquez-De Lucio 1, Edna María Hernández-Domínguez 1, Matilde Villa-García 1, Gerardo Díaz-Godínez 2, Virginia Mandujano-Gonzalez 3, Bethsua Mendoza-Mendoza 4 and Jorge Álvarez-Cervantes 1,* 1 Cuerpo Académico Manejo de Sistemas Agrobiotecnológicos Sustentables, Posgrado Biotecnología, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, Mexico; [email protected] (B.S.V.-D.L.); [email protected] (E.M.H.-D.); [email protected] (M.V.-G.) 2 Centro de Investigación en Ciencias Biológicas, Laboratorio de Biotecnología, Universidad Autónoma de Tlaxcala, Tlaxcala 90000, Tlaxcala, Mexico; [email protected] 3 Ingeniería en Biotecnología, Laboratorio Biotecnología, Universidad Tecnológica de Corregidora, Santiago de Querétaro 76900, Querétaro, Mexico; [email protected] 4 Instituto Tecnológico Superior del Oriente del Estado de Hidalgo, Apan 43900, Hidalgo, Mexico; [email protected] * Correspondence: [email protected]; Tel.: +52-771-5477510 Abstract: Enzymes are widely used in the food industry. Their use as a supplement to the raw Citation: Velázquez-De Lucio, B.S.; material for animal feed is a current research topic. Although there are several studies on the Hernández-Domínguez, E.M.; application of enzyme additives in the animal feed industry, it is necessary to search for new Villa-García, M.; Díaz-Godínez, G.; enzymes, as well as to utilize bioinformatics tools for the design of specific enzymes that work in Mandujano-Gonzalez, V.; certain environmental conditions and substrates. This will allow the improvement of the productive Mendoza-Mendoza, B.; Álvarez-Cervantes, J.
    [Show full text]
  • 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.
    [Show full text]
  • Biochemical Characterization of Digestive Carbohydrases in the Rose Sawfly, Arge Rosae Linnaeus (Hymenoptera: Argidae)
    J. Crop Prot. 2013, 2 (3): 305-318 ______________________________________________________ Biochemical characterization of digestive carbohydrases in the rose sawfly, Arge rosae Linnaeus (Hymenoptera: Argidae) Moloud Gholamzadeh Chitgar1, Seyed Mohammad Ahsaei2, Mohammad Ghadamyari1*, Mahbobe Sharifi1, Vahid Hosseini Naveh2 and Hadi Sheikhnejad1 1. Department of Plant Protection, Faculty of Agricultural Science, University of Guilan, Rasht, Iran. 2. Department of Plant protection, Faculty of Agricultural Sciences & Engineering, College of Agriculture and Natural Resources, University of Tehran, Karaj, Iran. Abstract: The rose sawfly, Arge rosae Linnaeus, is one of the most destructive pests of rose bushes in the north of Iran. Nowadays, many attempts have been made to reduce pesticide application by looking for new methods of pest control. A non chemical method for controlling insect pests including A. rosae can be achieved by using genetically engineered plants expressing carbohydrase inhibitors. Therefore, in present study we characterized biochemical properties of digestive carbohydrases in the gut of A. rosae for achieving a new method for control of this pest. The specific activity of α-amylase in the digestive system of last larval instars of A. rosae was obtained as 9.46 ± 0.06 μmol min-1 mg-1 protein. Also, the optimal pH and temperature for α-amylase were found to be at pH 8 and 50 °C. As calculated from Lineweaver-Burk plots, the Km and Vmax values for α-amylase were 0.82 mg/ml and 7.32 µmol min-1 mg-1 protein, respectively, when starch was used as substrate. The effects of ions on amylolytic activity showed that Mg2+ and Na+ significantly increased amylase activity, whereas SDS and EDTA decreased the enzyme activity.
    [Show full text]
  • The Mechanism of Carbohydrase Action 5
    246 Biochem. J. (1960) 76, 246 The Mechanism of Carbohydrase Action 5. ACTION OF HUMAN SALIVARY a-AMYLASE ON AMYLOPECTIN AND GLYCOGEN* By P. J. P. ROBERTSt AND W. J. W-HELANt Chemistry Department, University College of North Wales, Bangor (Received 11 January 1960) When human salivary oc-amylase acts on whole if any, esterified phosphorus (Schoch, 1953). It was pre- starch (amylose+amylopectin) there is produced pared from hand-sorted single-cross Tapicorn seed, (Bear a mixture of fermentable and unfermentable Hybrid Co., Decatur, Illinois, U.S.A.) as by Schoch (1957). sugars (Myrback, 1948). The fermentable sugars Buffers. These were 0-2 m-sodium acetate-acetic acid consist of maltose, maltotriose and/or glucose (see (pH 7.0) and 0-2M-sodiunm citrate-citric acid (pH 7-0). below). The non-fermentable sugars (a-limit Methods dextrins) are a mixture of higher oigosaccharides. Digests. Waxy-maize starch was moistened with ethanol Since the amylose component of starch, which and dissolved in 0-6N-sodium hydroxide by heating in a consists essentially only of 1:4-linked a-glucose boiling-water bath for 5 min. After cooling, the alkali was units, can be converted by the amylase completely neutralized to phenolphthalein either with sulphuric acid into maltose and maltotriose (Whelan & Roberts, [digests (1) and (2), see below] or hydrochloric acid [digest 1953) the a-limit dextrins must arise from the (3)]. Glycogen and the enzymes were dissolved in water. amylopectin component and may be assumed to After the substrate had dissolved, the buffer was added and contain the a-1:6-bonds which constitute the points then the enzyme.
    [Show full text]
  • Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms In
    CORE Metadata, citation and similar papers at core.ac.uk Provided by Texas A&amp;M Repository EXPERIMENTAL THERAPEUTICS crossm Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms in Wounds Downloaded from Derek Fleming,a,b Laura Chahin,a* Kendra Rumbaugha,b,c Departments of Surgerya and Immunology and Molecular Microbiologyb and TTUHSC Surgery Burn Center of Research Excellence,c Texas Tech University Health Sciences Center, Lubbock, Texas, USA ABSTRACT The persistent nature of chronic wounds leaves them highly susceptible to invasion by a variety of pathogens that have the ability to construct an extracel- Received 15 September 2016 Returned for lular polymeric substance (EPS). This EPS makes the bacterial population, or biofilm, modification 15 October 2016 Accepted 15 November 2016 up to 1,000-fold more antibiotic tolerant than planktonic cells and makes wound Accepted manuscript posted online 21 healing extremely difficult. Thus, compounds which have the ability to degrade bio- November 2016 http://aac.asm.org/ films, but not host tissue components, are highly sought after for clinical applica- Citation Fleming D, Chahin L, Rumbaugh K. tions. In this study, we examined the efficacy of two glycoside hydrolases, ␣-amylase 2017. Glycoside hydrolases degrade polymicrobial bacterial biofilms in wounds. and cellulase, which break down complex polysaccharides, to effectively disrupt Antimicrob Agents Chemother 61:e01998-16. Staphylococcus aureus and Pseudomonas aeruginosa monoculture and coculture bio- https://doi.org/10.1128/AAC.01998-16. films. We hypothesized that glycoside hydrolase therapy would significantly reduce Copyright © 2017 American Society for EPS biomass and convert bacteria to their planktonic state, leaving them more sus- Microbiology.
    [Show full text]
  • The Physiology and Biochemistry of the Digestion System of Termites from the Genus Anacanthotermes Jacobson, 1904
    International Journal of Biology; Vol. 11, No. 4; 2019 ISSN 1916-9671 E-ISSN 1916-968X Published by Canadian Center of Science and Education The Physiology and Biochemistry of the Digestion System of Termites from the Genus Anacanthotermes Jacobson, 1904 Ikram I. Abdullaev1, Manzura B. Doschanova1, Zafar Sh. Matyakubov2, Abdulla I. Iskandarov2, & Feruza R. Rakhimbaeva2 1 Khorezm Academy of Mamun, Khiva, Uzbekistan 2 Urgench State University (UrSU), Urgench, Uzbekistan Correspondence: Ikram Abdullaev, Chairman Khorezm Academy of Mamun, 220900, Khiva, Uzbekistan. Tel: 998-362-375-8051. E-mail: [email protected] Received: June 12, 2019 Accepted: July 5, 2019 Online Published: July 9, 2019 doi:10.5539/ijb.v11n4p1 URL: https://doi.org/10.5539/ijb.v11n4p1 Abstract A variety of morphological and functional features of the digestive system of termites is associated with their nutritional adaptation. Wood is mostly the food of termites’ adult larvae, workers and young nymphs. The salivary and intestinal enzymes play an important part in this process. The physiology and biochemistry of the digestion system of termites from the genus Anacanthotermes is still not fully studied. In the present research, we studied the activity of some carbohydrases in termites’ salivary glands. Our data show that the activity of exocellulase in adult termites is 1.5 times more that in young individuals and 3 times more active than in nymphs, while the exocellulase in soldiers remains inactive. Moreover, the activity of celluloses in the intestine of A. turkestanicus is still not fully studied. We observed that exocellulase is involved in the digestion of food polymers in the castes of termites-workers, nymphs and soldiers.
    [Show full text]
  • KS3 Science Textbook Sample
    Contents Enquiry processes 6 More on planning how to answer a question 2 10 Critique claims and justify opinions 10 7 More on analysing and evaluating 4 11 Risks and benefits 12 8 Communication 6 12 Review theories 1 14 9 Evidence and sources 8 13 Review theories 2 16 1: Forces Part 2 Opener 18 1.3 Contact forces 1.4 Pressure 1.3.1 Friction and drag 20 1.4.1 Pressure in gases 26 1.3.2 Squashing and stretching 22 1.4.2 Pressure in liquids 28 1.3.3 Turning forces 24 1.4.3 Stress on solids 30 Part 2 Summary and Questions 32 2: Electromagnets Part 2 Opener 34 2.3 Magnetism 2.4 Electromagnets 2.3.1 Magnets and magnetic fields 36 2.4.1 Electromagnets 38 2.4.2 Using electromagnets 40 Part 2 Summary and Questions 42 3: Energy Part 2 Opener 44 3.3 Work 3.4 Heating and cooling 3.3.1 Work, energy, and machines 46 3.4.1 Energy and temperature 48 3.4.2 Energy transfer: particles 50 3.4.3 Energy transfer: radiation and insulation 52 Part 2 Summary and Questions 54 4: Waves Part 2 Opener 56 4.3 Wave effects 4.4 Wave properties 4.3.1 Sound waves, water waves, and energy 58 4.4.1 Modelling waves 62 4.3.2 Radiation and energy 60 Part 2 Summary and Questions 64 5: Matter Part 2 Opener 66 5.3 Elements 5.4 Periodic Table 5.3.1 Elements 68 5.4.1 The Periodic Table 78 5.3.2 Atoms 70 5.4.2 The elements of Group 1 80 5.3.3 Compounds 72 5.4.3 The elements of Group 7 82 5.3.4 Chemical formulae 74 5.4.4 The elements of Group 0 84 5.3.5 Polymers 76 Part 2 Summary and Questions 86 ii 6: Reactions Part 2 Opener 88 6.3 Types of reaction 6.4 Chemical energy 6.3.1 Atoms
    [Show full text]
  • Carbohydrase and Phytase Supplementation in Diets for Semi-Heavy Laying Hens
    Acta Scientiarum http://www.uem.br/acta ISSN printed: 1806-2636 ISSN on-line: 1807-8672 Doi: 10.4025/actascianimsci.v36i3.21952 Carbohydrase and phytase supplementation in diets for semi-heavy laying hens Adriano Geraldo1*, Karina Rodrigues Aurora Gomes1, Édison José Fassani2, Antonio Gilberto Bertechini2, Sérgio Domingos Simão1 and Filipe Soares Nogueira1 1Departamento de Ciências Agrárias, Instituto Federal de Educação Ciência e Tecnologia de Minas Gerais, Fazenda Varginha, km 05, Rodovia Bambuí-Medeiros, Cx. Postal 05, 38900-000, Bambuí, Minas Gerais, Brazil. 2Departamento de Zootecnia, Universidade Federal de Lavras, Lavras, Minas Gerais, Brazil. *Author for correspondence. E-mail: [email protected] ABSTRACT. This study was conducted in order to evaluate the association of phytase with an enzymatic complex comprised of carbohydrases (α-galactosidase, galactomannan, xylanase and β-glucanase) in nutrition reduction diets for semi-heavy laying hens and its effect on egg performance and egg quality. Four hundred Isa Brown laying hens with 42 to 57 weeks of age were distributed in an entirely random experiment with five treatments and 8 repetitions, during five production periods of 21 days. Variables studied: egg production, feed intake, mean egg weight, feed conversion, Haugh unit, percentage of yolk, egg white and albumen, yolk color, eggshell thickness and specific gravity. There was a significant interaction (p < 0.05) between treatments and experimental periods for feed intake. There were no significant effects (p > 0.05) of treatment on production, egg weight or internal and external egg quality. Treatment effects on feed conversion showed better values for hens fed with the control diet. The levels of nutrient reduction used in the diets with or without enzyme supplementation did not provide good results with regard to feed conversion and feed intake.
    [Show full text]
  • Production of Dextrose and Maltose Syrups Using an Enzyme Derived from Rice
    Europaisches Patentamt J European Patent Office © Publication number: 0 127 291 Office europeen des brevets A1 (12) EUROPEAN PATENT APPLICATION @ Application number: 84302289.8 © Int. CI.3: C 12 P 19/20 C 12 P 19/22 © Date of filing: 04.04.84 © inventor: © Priority: 20.05.83 US 496386 Line, William F. 5200 S. Tuckaway Blvd. Greenfield Wisconsin 53221 (US) © of of Date publication application: © 05.12.84 Bulletin 84/49 Inventor: Chaudhary, Vinod K. 9496 North Green Bay Road Brown Deer Wisconsin © Designated Contracting States: 53029(US) DE FR GB @ Inventor: Chicoye, Etzer © Applicant: Miller Brewing Company 4374 N. Menomonee River Parkway Milwaukee 3939 W. Highland Boulevard Wisconsin 53225(US) Milwaukee Wisconsin 53223(US) © Inventor: Mizerak, Robert J. N8 3071 0 Cherokee Trail Waukesha Wisconsin 531 86(US) © Representative: Wynne-Jones, John Vaughan et al, Wynne-Jones, Laine & James 22, Rodney Road Cheltenham Gloucestershire GL50 1 JJ(GB) © Production of dextrose and maltose syrups using an enzyme derived from rice. ©A A sugar syrup is prepared by saccharifying a thinned starch hydrolyzate at a pH of about 4.5 to about 7 and a temperature above about 45°C with a heat-stable pullulanase obtained from rice, and an @-1,4a-1,4 carbohydrase.Thecarbohydrase. The pullulan- ase employed is free of maltase and transglucosidase activities. In a preferred embodiment, a dextrose syrup is prepared by saccharifying the thinned starch hydrolyzate with glucoamylase and the rice debranching enzyme at a pH of about 5 and at a temperature of about 55°C. A method of preparing a maltose syrup using the rice debranching enzyme is also disclosed.
    [Show full text]
  • Malt Carbohydrase
    MALT CARBOHYDRASE Prepared at the 15th JECFA (1971), published in NMRS 50B (1972) and in FNP 52 (1992). An ADI 'not limited' was established at the 15th JECFA (1971) SYNONYMS Malt SOURCES Malt is the product of controlled germination of barley Active principles 1. alpha-Amylase (glycogenase, diastase) 2. ß-Amylase (glycogenase, diastase) Systematic names and 1. 1,4-alpha-D-Glucan glucanohydrolase (EC 3.2.1.1) numbers 2. 1,4-alpha-D-Glucan maltohydrolase (EC 3.2.1.2) Reactions catalyzed 1. Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides, (starch, glycogen) yielding dextrins and oligo- and monosaccharides. 2. Hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides, (starch, glycogen) yielding successively maltose units from the non-reducing ends of the chains. FUNCTIONAL USES Enzyme preparation Used in brewing, baking, manufacture of alcoholic beverages and manufacture of syrups. GENERAL Must conform to the General Specifications for Enzyme Preparations used SPECIFICATIONS in Food Processing (see Volume Introduction) CHARACTERISTICS IDENTIFICATION alpha-Amylase activity The sample shows alpha-amylase activity (Vol. 4) alpha- and ß-amylase The sample shows Diastatic power activity See description under TESTS TESTS IDENTIFICATION TESTS Diastatic power Determination of a diastatic power of malt (combined activity of alpha- and ß-amylase) according to Amer. Soc. Brewing Chem., 6th ed., 162 (1958). Reagents For Digestion of Starch Solution - Acetate buffer solution: Dissolve 68 g of sodium acetate (CH3COONa · 3H2O), reagent grade, in 500 ml of one N acetic acid and make the solution up to one litre with distilled water. - Sodium hydroxide solution: 0.5 N - Special starch: Starch manufactured specifically for diastatic power determination is available from Merck & Co., Rahway, New Jersey.
    [Show full text]