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An Acylase System of Lactobacillus Arabinosus Robert Worth Park Iowa State College

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An Acylase System of Lactobacillus Arabinosus Robert Worth Park Iowa State College Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1953 An acylase system of Lactobacillus arabinosus Robert Worth Park Iowa State College Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons Recommended Citation Park, Robert Worth, "An acylase system of Lactobacillus arabinosus " (1953). Retrospective Theses and Dissertations. 12407. https://lib.dr.iastate.edu/rtd/12407 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced fronn the microfilm master. UMl films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMl a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overiaps. ProQuest Information and Learning 300 North Zeeb Road, Ann Arbor, Ml 48106-1346 USA 800-521-0600 NOTE TO USERS This reproduction is the best copy available. UMI' ii.N ACYLASt SYSTEf. OF LACTOBACILLUS ARAEIN0£US by Robert '''orth Park A Dissertation Jrubmitted to the Graduate Faculty in Partial Fulfillrrent of The Requirements for the Degree of DOCTOR OF PHILOSOPHY Kajor Subject: Bl,o<ihe£ni'5try Approved: Signature was redacted for privacy. In Charge of^Major '-.'ork Signature was redacted for privacy. Head of Major Dep^rtnfent Signature was redacted for privacy. De#n of Graduate College Iowa Stste College 1953 UMI Number: DP11806 UMI UMI Microform DP11806 Copyright 2005 by ProQuest Information and Learning Company. All rights reserved. This microform edition is protected against unauthorized copying under Title 17, United States Code. ProQuest Information and Leaming Company 300 North Zeeb Road P.O. Box 1346 Ann Arbor, Ml 48106-1346 - 11 - TABLE OF CONTZNTS Page I. INTRODUCTION 1 A. Delineation of Subject 1 B. Objectives 1 II. HISTORICAL 5 A. Terminology 5 1. Acylase 5 2. Hietozyme 7 3. Hlppuricase 8 4. Carboxyper-tldaee 8 5. Aminoacylase 9 B. Llmitatione of Enzyme Studies 9 C. Acylaeee Found in Anlmale and slants 11 1. Acylases of InvertebreteB 12 a. Crlbrina artemlsia 12 b. A carnivorous species of Platyhelmlnthes (flattened worms) 12 c. A blood-consuming Platyhelmlnthes 12 d. Moniezie benedeni 13 e. MaJa squinado 13 f. The fresh-vater flea Daohnla 13 g* Tridacna elongata 13 h. Helix pomatia 13 2. Acylases of vertebrates 14 a. Pacific Coast King Salmon 14 b. Ophlocephalue tadlana 14 c. Na.la na.la (cobra), Vlpera ruBsellil. and B. fasciatus 15 d. Echis carinata 15 e. The chicken 15 f. The pigeon 15 g. The dog 16 h. The cat 33 1. The guinea pig 3^ - ill - Page J. The mouse 35 k. The rat 38 1. The rablDit 39 m. The sheep 5^ n. The cow 5^ 0. The hog 75 p. The horse 138 q. Man 1^0 3. Acylases of algae 1^5 a. Spirogyra 1^5 Acylasee of bacteria (Phylum schlzomycophyta) 1^5 a. Some species of water vibrio 1^6 b. Staphylococcus aureus 1^7 c. Staphylococcus pyi*ogenes citreus Nr. 1 150 d. A strain of Staphylococcus from bubo 150 e. Soil bacteria KT 1, KT 3, KT 4, KT 9, KT 13, KT 17, KT 2, KT 6, and KT 7 150 f. Streptococcus faecalis. Leuconostoc mesenteroides. Leuconostoc citrovorum. Lactobacillus arabinoetie. Lactobfecillus brevis. Lactobacillus easel, and Lactobacillus pentoacetacus 151 gi Escherichia coli 162 h. Proteus OX 19 164 1. Bacillus tynhi. Bacillus dysentheriae. Bacillus enterdltis Gartneri. Bacillus paratyr^hi A and B, and "Sarcina" 164 J* Bacillus prodigioBus. Bacillus proteus. Bacillus subtilia. Bacillus pyoceneus 164 k. Mycobacterium phlei 167 5. Acylases of true fungi (Phylum eumycophyta) 168 a. Saccharomyces cerevisiae 168 b. Penicillium notatum 17^ 169 c. Aspergillus niger 169 d. Aspergillus oryzae 172 e. Penicillium NBRL 1978 Bo and Penicillium 176 Yabuta 173 - Iv - Page T. Aspergillus clevatue. Aspergillus fumig&tus. Penlclllium eypansum. Penicilllum roouefortl. Penlclllium cfiJBembertl. Penlclllium chrysogenum. Penlclllium brevlcaule. Penlclllium glaucum, Cltromyces glaber, Rhlzopus tonkinensls. Mucor circinellordes. cladosporium herbamm. Fuearlum oxysporlum. Monascus pxirpureus. Butrytig stroph&noderie 173 g. Cltromyces glaber and Cltromyces pfefferlanus 176 h. Aspergillus parasiticus 178 Mortierells renispora PRL 26, G-llocladlum roseum PRL 79i Gllocladlum roseum PRL M. Trlchoderma vlrlde PRL 92, Fusarlum sp. PRL 232, Chaetomlum sp. PRL 319# Aiternaria tenuis PRL 369i and Streptomyces sp. PRL 376 178 6. Acylaees of vascular lants (Phylum trocheophyta) I78 a. Oats and barley I78 b. Carlca papaya 180 c. Tomato plant 181 III. EXPERIMENTAL PROCEDURES 184 A. Preparation of Compounds 184 1, Compounds previously reported but synthesized by new or modified procedures 184 a. Copper l-amlnocyclobutsne carboxylate 184 b. 1-Amlnocyclobutane carboxylic acid 185 c. Benzoyl-Jpleuclne 186 d. Jf-leuclne methyl ester 189 2. New compounds 191 a. N-phenylacetyl-l-amlnocyclobutane carboxylic acid 191 b. N-Benzoyl-l-amlnocyclobutane carboxylic acid 191 V - Page 3. Known compounds eynthesized as described In the literature 192 B. Compounds Received as G-lfts or Purch-ased from Commercial Sources 192 C. General Bacteriological Procedure 198 1. Bacterial cultures 198 2. Preparation of inocula 199 3. Media 200 4. General assay procedures 206 D. Enzyme Studies 209 1. Enzyme preparations 209 a. In solution with acetate, phosphate, end metal salts 209 b. Enzyme Preparation II (lyophilized) 213 c. Enzyme Preparation III A and III B {lyophilized) 219 2. Enzyme-substrate Incubrtlone 219 3* Assays for liberated amino adds 224 a. General 224 b. Effect of substrates, substrate oroducts, buffers, enzyme preparations and potential inhibitors on accuracy of assays 224 E. Utilization Exrjerlments 226 F. Growth Inhibition Experiments 227 IV. EXPERIMENTAL RESULTS . 229 A. Utilization Experiments 229 B. Effect of Enzyme Substrates and Substrate Products on Amino Acid Assays 233 C. Hydrolysis of Various Acylamlno Acids by Enzyme Preparations from Lactobacillus arablnosue 234 1. Acylase activity of Enzyme Preparation I 23^ 2. The acylase activity of Enzyme Preparation II 235 a. Acylase activity on various acylamlno acids over a pH range 235 - vi - Page b. Relative rates of hydrolysis of various acylamino acids by Enzyme Preparation II and pH optima 262 3. The acylase activity of Enzyme Preparation III A and III B 266 a. Hydrolysis of benzoyl-L-leucine and carbobenzoxyglycyl-^leucine 266 b. Recovery of acylase activity in prepara­ tion of alcohol precipitated and lyophilized preparation 267 4. Acylase activity of cell susnensions 268 D. The Effect of Various Compounds on Hydrolysis by Acylase 269 E. The Effect of Isocanroate on the Growth of Lactobacillus arabinosus 269 V. DISCUSSION 273 A. Characteristics of the Acylase System of Lactobacillus arabinosus and Comparison with Other Acylases 273 1. Substrate oreferences of the acylase system of Lactobacillus arabinosus 273 2. Comparison of the substrate preferences of Lactobacillus arabinosus acylase with the acylases from other sources 3. Comparison of acylase inhibition patterns 281 hr, pH and acylase activity 282 5. Enzymes present in the acylase system of Lactobacillus arabinosus 284 B. Relationships between Behaviour of Acylases and Cellular Behavior 285 1. The relation between Lactobacillus arabinosus acylase hydrolysis and utilization of acylamino acids by Lactobacillus arabinosus 285 2. Cell environment and acylase activity 28? 3. Role of Lactobacillus arabinosus acylase in cellular metabolism 290 - vil - Page a. Ae digestive enzyme 291 "b. In protein synthesis 291 C. Comment on Ext)erimental Methods Used in Enzyme Studies 315 VI. SUMMARY AND CONCLUSIONS 318 VII. ACKNOWLEDGMENTS 322 - 1 - I. D^TEODUCTION A. Delineation of Subject An acylase is an enzyme vhlch catalyzes the hydrolysis of acylamino acids; that is, speeds up the following reaction: R • - CO- NH- CHR- COOH +H2O ^ R • - C OOH -f NH3- C HR- COO" This thesis describes an investigation of the properties end possible physiological importance of an acylase or acylasee from the acid producing bacterium, Lactobacillus arabinosus. B. Objectives Itschner 1, Drechsler 2, Fox and ^'-'arner-'^ have shown that K. F. Itschner. Bacterial utilization and sequence determination of peptides. Unpublished Ph.D. Thesis. Ames, Iowa, Iowa State College Library. 1951 2E. R. Drechsler. Utilization of certain benzoylamlno acids by several species of bacteria. Unpublished M.S. Thesis. Ames, Iowa, Iowa State College Library. 1952. ^S. Fox and C. W. Warner state, on the basis of un­ published exneriments, thst benzoyl-£J^-methionine is r.ertially utillzable for the methionine
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