DOCSLIB.ORG

Production and Optimization of Alkaline Protease by Bacillus Spp

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Production and Optimization of Alkaline Protease by Bacillus Spp Imperial Journal of Interdisciplinary Research (IJIR) Vol-3, Issue-11, 2017 ISSN: 2454-1362, http://www.onlinejournal.in Production and Optimization of Alkaline Protease by Bacillus spp. Isolated from Tannery Industry and Potential Biotechnological Application of the Enzyme Tahsin Khan* & Mihir Lal Saha Laboratory of Microbiology, Department of Botany, University of Dhaka, Dhaka- 1000, Bangladesh Abstract: Four Bacillus spp. strains isolated from the enzyme market most of which are alkaline proteases effluents of tannery industries (Dhaka, Bangladesh) [5]. Most commercial alkaline proteases are showing proteolytic activity were studied to produced by bacteria, especially Bacillus spp. [1] for determine their alkaline protease enzyme production several reasons, including their high growth rates capability. They were also optimized with respect to leading to short fermentation cycle time, initial medium pH and temperature. Their range of accompanied with extracellular secretion of enzymes enzyme activity were between 47.84 and 179.13 [6, 7]. U/ml, initially. The optimum initial media pH was Detergent industries are the primary consumers of 10.0 for B. subtilis B20, 9.0 for both B. subtilis PB18 enzymes, in terms of both volume and value [8]. The and Bacillus sp. BVC38 and 7.0 for B. use of enzymes in detergent formulations enhances amyloliqefaciens Egy25. Optimum temperatures the detergents’ ability to remove tough stains making were determined as 60° C for both B. subtilis B20 the detergent environmentally safe also. Nowadays, and PB18 and 40 °C for the other two organisms. many laundry-detergents contain cocktails of After optimization, alkaline protease production enzymes including proteases, amylases, cellulases capability of B. subtilis B20 and PB18 was increased and lipases. Microbial proteases, have major to 301.80 and 255.34 U/ml, respectively. The crude application in detergent formulations [9, 10]. enzyme of B. subtilis B20 with better wash Proteases also help to prevent the redeposition of performance analysis (visually) and an optimum pH proteins on fabrics, particularly hydrophobic ones 10.0 and 60° C temperature can be considered as a such as blood, thereby also providing a whiteness potential candidate for biotechnological application benefit [11]. Alkaline proteases with superior in detergent industry. The crude alkaline proteases performance for commercial exploitations, especially produced by the four organisms were also tested for for detergents, are being sought. Although such their dehairing potentiality of raw hides and enzymes enzymes have already been found in some strains of from B. subtilis B20 and PB18 showed better results Bacillus proteolyticus, B. thermantarcticus, and B. of dehairing like lime-sulphide chemical treatment, mojavensis [12-14], further exploration of protease which can be considered as environment friendly producers is warranted. alternative to the hazardous chemical treatment in Alkaline proteases are envisaged to have tannery industries. extensive applications in leather industries. The enzymes catalyze the breakdown of the protein Keywords: Alkaline protease; Bacillus spp.; keratin in the hair and allow it to be easily removed. detergent additive; dehairing agent. In a tannery, rawhides are subjected to series of chemical treatments prior to tanning and are 1. Introduction converted to finished leather. Proteases may play a vital role in these treatments by replacing these Proteases or proteinases are proteolytic enzymes hazardous chemicals especially involved in soaking, which catalyze the hydrolysis of proteins. Proteases dehairing and bating [15]. The conventional method have wide applications in leather processing, for depilation has now been clearly recognized to be detergent, food, pharmaceutical, and textile environmentally objectionable accounting for the industries [1, 2]. Proteases can be obtained from discharge of 100 % of sulfide and 80 % of the plants, animal organs and microorganisms, but the suspended solids in the tannery effluent [16]. But the application of bacterial proteases is more significant advantage of using proteases for dehairing of skins when compared to the proteases from other sources are the reduction of the sulfide contents in the [3]. Selection of the right organism plays a key role effluent, recovery of the hair/wool which is of good in obtaining high yield of desirable enzymes. Besides quality, an increased yield of leather area, easy the cultural parameters like temperature and pH also handling of the pelts by workmen, simplification of plays a major role in enzyme production [4]. the pretreatment, the elimination of the bate in the Proteases constitute 60–65% of the global industrial deliming stage and finally the production of a good Imperial Journal of Interdisciplinary Research (IJIR) Page 258 Imperial Journal of Interdisciplinary Research (IJIR) Vol-3, Issue-11, 2017 ISSN: 2454-1362, http://www.onlinejournal.in quality pelts/leather [17, 18]. Usage of enzymes for M Tris-HCl buffer was incubated with 400 μl of dehairing and bating not only prevents pollution crude enzyme for 60 min at 40 °C. The reaction was problems, but also is effective in saving energy. In stopped by the addition of 135 μl of 35% general, proteases play a vital role in leather trichloroacetic acid (TCA) keeping the mixture for processing starting from soaking of hides to finished 10 min at 4° C. After centrifugation at 13,000 rpm products [19, 20]. for 10 min 750 μl of supernatant was mixed with 750 Therefore, taking the demands into account and μl of 1 N NaOH and then absorbance was taken at knowing the geographic richness and biodiversity of 440 nm. The control was prepared by adding TCA our local environment, it was assumed that there is before the addition of enzyme in substrate. One unit potential for alkalophilic Bacillus spp. strains living of protease activity was determined as the amount of here. Discovering such strains and producing enzyme that produces an increase in absorbance of alkaline proteases with novel characteristics will be 0.01 under the above assay condition. of great value to the enzyme industry for different applications. With this as main objective, the 2.4. Characterization of the Crude Protease effluents of Hazaribagh tannery industries were Enzyme screened for isolating bacterial strains of interest and four potential proteolytic Bacillus sp. were found The crude proteases obtained from the four [21]. In this study, the goal was to estimate alkaline organisms were further subjected to preliminary protease enzyme production capability of the characterization study. Therefore, the effects of organisms regarding temperature and pH initial media pH and temperature on their activity optimization. Also, to exploit the potentiality of the were studied. The procedures are outlined below. crude enzymes as detergent additive and dehairing agent of rawhide. 2.4.1. Effect of Initial Media pH on Activity of Protease 2. Materials and Methods The effect of initial media pH on the proteolytic 2.1. Microorganism activity of crude alkaline proteases from the four Bacillus spp. were determined by assaying the Four proteolytic Bacillus sp. were isolated from enzyme activity at different pH values ranging from the effluents of leather processing industries and 7.0 to 12.0 using the following buffer systems: identified as B. subtilis B20, B. subtilis PB18, phosphate (pH 7.0), Tris-HCl (pH 8.0-9.0), glycine- Bacillus sp. BVC38 and B. amyloliqefaciens Egy25 NaOH (pH 10.0–11.0) and KCl-NaOH (pH 12.0) at [21]. 40° C and under standard assay conditions. The concentration of each buffer was 0.1 M. The relative activities were based on the ratio of the activity obtained at certain pH to the maximum activity 2.2. Media and Culture Conditions obtained at that range and expressed as percentage considering 0.5 % error. Seed culture for the experiment was prepared in a test tube containing 5 ml of nutrient broth medium 2.4.2. Effect of Temperature on Activity of (pH 8.0) by inoculating with one bacterial colony Protease from fresh culture and incubating at 37 °C for 24 h. 5 ml of seed culture was transferred aseptically to a The effect of temperature was determined by 250-ml conical flask containing 50 ml of modified incubating the reaction mixture (keeping the different alkaline protease producing broth (APPB) medium optimum pH for each organism) for 60 min at [22] consisting of 1% glucose, 0.5% peptone, 0.5% different temperatures ranging from 20 to 80° C (at yeast extract, 0.5% K2HPO4, 0.01% MgSO4.H2O and 20° C intervals) and under standard assay conditions. pH 8.5. The flask was then incubated in a rotary The relative activities (as % considering 0.5% error) shaker incubator at 40° C for 48 h at 150 rpm. After were expressed as the ratio of the proteolytic activity 48 h, the culture fluid was withdrawn and obtained at certain temperature, to the maximum centrifuged at 8000 rpm for 10 min at 4° C. The cell activity at the given temperature range. free supernatant was used for crude enzyme assay. 2.5. Evaluation of Washing Performance 2.3. Assay for Proteolytic Activity Clean cotton cloth was soiled with fresh bovine Protease activity was determined with azo-casein blood and dried overnight. Small pieces (5cm x 5cm) (Sigma Co. St. Louis Mo), according to the modified were cut from the cloth. The stained cloth pieces procedure described by Kreger and Lockwood [23]. were subjected to wash treatments with commercial In this method, 400 μl of azo-casein solution in 0.05 solid detergent (Jet, local detergent powder available Imperial Journal of Interdisciplinary Research (IJIR) Page 259 Imperial Journal of Interdisciplinary Research (IJIR) Vol-3, Issue-11, 2017 ISSN: 2454-1362, http://www.onlinejournal.in in Bangladesh market) diluted in tap water at 7 activity of PB18 was raised to 255.3 U/ml, which mg/ml, supplemented with and without crude was second highest among the four. enzyme. The stained cloth pieces were taken in separate flasks, with 100 ml as final volume, as mentioned above: flask with tap water only; flask with tap water and only commercial detergent (Jet) at final concentration of 7 mg/ml and flask with tap water commercial detergent and crude enzyme (10 ml).
Load more

Recommended publications
  • Revision of Ecolabel Criteria for Laundry Detergents 2008-2010
    European Ecolabel ENV.G.2/SER2007/0073rl Commission Decision of 28 April 2011 Revision of Ecolabel Criteria for Laundry Detergents 2008-2010 Background report Prepared by Ecolabelling Denmark This document was last updated February 2011 INDEX 1. SUMMARY ....................................................................... 2 2. MARKET REVIEW ............................................................. 4 2.1. EUROPEAN MARKET FOR LAUNDRY DETERGENTS AND ADDITIVES .................................... 4 2.1.1. Laundry detergents .............................................................................................. 4 2.1.2. Fabric softeners ..................................................................................................... 5 2.1.3. Stain Removers ...................................................................................................... 6 2.2. WASHING HABITS IN EUROPE ............................................................................................. 6 2.3. ECOLABEL LICENSES AND PRODUCTS TODAY ..................................................................... 6 3. PRODUCT GROUP DEFINITION ........................................ 8 4. INTRODUCTION TO REVISED ECOLABEL CRITERIA ....... 10 5. REVISED ECOLABEL CRITERIA ...................................... 13 5.1. REVISED CRITERIA ............................................................................................................. 13 5.1.1. General remarks .................................................................................................
    [Show full text]
  • Risk Assessment Guidance for Enzyme-Containing Products
    Risk Assessment Guidance for Enzyme-Containing Products The Soap and Detergent Association Table of Contents Preface 2 Executive Summary 3 Chapter 1 — Introduction to Enzymes 4 Chapter 2 — Introduction to Risk Assessment 6 Chapter 3 — Hazard Identification 8 Chapter 4 — Dose-Response Assessment 11 Chapter 5 — Exposure Assessment 17 Chapter 6 — Risk Characterization 23 Chapter 7 — Risk Management 28 Chapter 8 — Conclusions 30 Bibliography 31 Glossary 38 Appendix 1 — Estimation of Exposure to Enzymes from Early Detergent Formulations 41 Appendix 2 — Enzyme Risk Assessments of Hand-Laundering Practices 51 Appendix 3 — Spray Pre-Treater Case Study 54 FIGURES — 1, 2, 3 A, 3 B, 4 TABLE — 1 Copyright © 2005:The Soap and Detergent Association. Al rights reserved. No part of this document may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or by any infor- mation storage retrieval system, without written permission from the publisher. For information, contact:The Soap and Detergent Association, 1500 K Street, NW, Suite 300,Washington, DC 20005, USA. Telephone: +1-202-347-2900. Fax: +1-202-347-4110. Email: [email protected]. Web: www.sdahq.org PREFACE he laundry product industry has implemented For additional information on risk assessment and Ta successful product stewardship program to risk practices for enzymes, contact your enzyme promote the safe use of enzymes in the workplace supplier, or and by users of their products,using both appropriate risk assessment and risk management practices. The Soap and Detergent Association Much of the information about enzymes for laundry 1500 K Street, NW, Suite 300 applications can be applied to other finished products Washington, DC 20005 including those in the cleaning and personal care Tel: 202-347-2900 markets.
    [Show full text]
  • Risk of Enzyme Allergy in the Detergent Industry
    Occup Environ Med 2000;57:121–125 121 Occup Environ Med: first published as 10.1136/oem.57.2.121 on 1 February 2000. Downloaded from Risk of enzyme allergy in the detergent industry Markku Vanhanen, Timo Tuomi, Ulla Tiikkainen, Outi Tupasela, Risto Voutilainen, Henrik Nordman Abstract sation to enzymes and the levels of exposure to Objectives—To assess the prevalence of protease in a detergent factory. enzyme sensitisation in the detergent industry. Material and methods Methods—A cross sectional study was DETERGENT FACTORY conducted in a detergent factory. Sensiti- The study was carried out in a factory produc- sation to enzymes was examined by skin ing laundry detergents and automatic dish prick and radioallergosorbent (RAST) washing detergents. The factory had been tests. 76 Workers were tested; 40 in manu- operating since the 1960s. New facilities were facturing, packing, and maintenance, and built in the mid-1980s. Detergents for laundry 36 non-exposed people in management and dish washing were produced in separate and sales departments. The workers were departments. The manufacturing of laundry interviewed for work related respiratory detergents includes mixing of raw materials and skin symptoms. Total dust concentra- with water and subsequent spray drying of the tions were measured by a gravimetric slurry, followed by addition of heat labile com- method, and the concentration of protease ponents such as enzymes. The addition of in air by a catalytic method. enzyme to the hopper took place manually a Results—Nine workers (22%) were sensi- few times in a shift. Further mixing to the tised to enzymes in the exposed group of detergent was automated.
    [Show full text]
  • Assessing the Risk of Type 1 Allergy to Enzymes Present in Laundry and Cleaning Products: Evidence from the Clinical Data
    Toxicology 271 (2010) 87–93 Contents lists available at ScienceDirect Toxicology journal homepage: www.elsevier.com/locate/toxicol Assessing the risk of type 1 allergy to enzymes present in laundry and cleaning products: Evidence from the clinical data Katherine Sarlo a,∗, Donald B. Kirchner a, Esperanza Troyano a, Larry A. Smith a, Gregory J. Carr a, Carlos Rodriguez b a The Procter & Gamble Company, Cincinnati, OH, United States b The Procter & Gamble Company, Brussels, Belgium article info abstract Article history: Microbial enzymes have been used in laundry detergent products for several decades. These enzymes Received 25 January 2010 have also long been known to have the potential to give rise to occupational type 1 allergic responses. A Received in revised form 22 February 2010 few cases of allergy among consumers using dusty enzyme detergents were reported in the early 1970s. Accepted 3 March 2010 Encapsulation of the enzymes along with other formula changes were made to ensure that consumer Available online 17 March 2010 exposure levels were sufficiently low that the likelihood of either the induction of IgE antibody (sensitiza- tion) or the elicitation of clinical symptoms be highly improbable. Understanding the consumer exposure Keywords: to enzymes which are used in laundry and cleaning products is a key step to the risk management pro- Enzymes Allergy cess. Validation of the risk assessment conclusions and the risk management process only comes with Asthma practical experience and evidence from the marketplace. In the present work, clinical data from a range IgE antibody of sources collected over the past 40 years have been analysed.
    [Show full text]
  • Combo Detergent Enzymes Types
    JIAAN Enzymes replacing Chemicals BIOTECH Biological washing pow- ders contain enzymes to help to re- move stains from clothes. They con- tain these enzymes: amylases DETERGENT (carbohydrases) - to digest starch. ENZYMES proteases - to digest protein and re- move protein stains (such as egg and blood) Most biological laundry deter- Combo Detergent gents contain lipase and protease enzymes, both of which are found in Enzymes Types: the body. Lipases break down fats and oils, while proteaseswork to JiaanD-Cocktail 1 break down protein chains. Their ability to break down the- JiaanD-Cocktail 2 se compoundsmakes them excel- JiaanD-Cocktail 3 lent for stain removal. J B HO - K T N P I MP F P N - S- A P MP E ID P - JIAAN ENZYMES - - Detergent Enzymes : Combo Packs These Enzymes are combination of various Enzymes , which are alternate to the traditional laundry detergents. Hence, these enzymes delivers powerful stain removal with the brilliance and fabric care benefits highly effective at the lower was temperature . Perfect Stain cleaning than the traditional chemical ingredients. 1. JiaanD-Cocktail 2 ADVANTAGES : Jiaan-D-Cocktail 2 is a combo of Protease, Lipase , Cellulase and Alpha amylase enzymes. Alternative to traditional laundry detergent, Jiaan-D- 1. Powerful stain cleaner than the traditional chemical Ingredients, removes Cocktail 2 delivers the powerful stain removal with the brilliance and fabric dirt & grease care benefits highly effective at the all wash temperature. Perfect stain clean- 2. Suitable with natural surfactants 3. Bio-based and readily bio-degradable ing than the traditional chemical ingredients. 4. Reduces the environmental load 5.
    [Show full text]
  • Novel Perspectives for Evolving Enzyme Cocktails for Lignocellulose
    Mohanram et al. Sustainable Chemical Processes 2013, 1:15 http://www.sustainablechemicalprocesses.com/content/1/1/15 REVIEW Open Access Novel perspectives for evolving enzyme cocktails for lignocellulose hydrolysis in biorefineries Saritha Mohanram, Dolamani Amat, Jairam Choudhary, Anju Arora* and Lata Nain Abstract The unstable and uncertain availability of petroleum sources as well as rising cost of fuels have shifted global efforts to utilize renewable resources for the production of greener energy and a replacement which can also meet the high energy demand of the world. Bioenergy routes suggest that atmospheric carbon can be cycled through biofuels in carefully designed systems for sustainability. Significant potential exists for bioconversion of biomass, the most abundant and also the most renewable biomaterial on our planet. However, the requirements of enzyme complexes which act synergistically to unlock and saccharify polysaccharides from the lignocellulose complex to fermentable sugars incur major costs in the overall process and present a great challenge. Currently available cellulase preparations are subject to tight induction and regulation systems and also suffer inhibition from various end products. Therefore, more potent and efficient enzyme preparations need to be developed for the enzymatic saccharification process to be more economical. Approaches like enzyme engineering, reconstitution of enzyme mixtures and bioprospecting for superior enzymes are gaining importance. The current scenario, however, also warrants the need for research and development of integrated biomass production and conversion systems. Keywords: Lignocellulose, Bioethanol, Cellulase, Hemicellulase, Bioprospecting, Enzymatic saccharification Introduction Investment into biofuels production capacity exceeded Increased public and scientific attention towards alterna- $4 billion worldwide in 2007 and is growing.
    [Show full text]
  • The Role of Enzymes in Modern Detergency
    REVIEW The Role of Enzymes in Modern Detergency Hans Sejr Olsen* and Per Falholt Enzyme Development & Application, Enzyme Business, Novo Nordisk A/S, DK-2880 Bagsvaerd, Denmark ABSTRACT: Enzymes have effectively assisted the develop- lulases, the foundations were already laid in 1913 for the ment and improvement of modern household and industrial de- commercial use of enzymes that continues to be important tergents. The major classes of detergent enzymes—proteases, li- today. pases, amylases, and cellulases—each provide specific benefits Today the most widely used industrial enzymes are hy- for application in laundry and automatic dishwashing. Histori- drolases, which remove soils based on proteins, lipids, and cally, proteases were first to be used extensively in laundry de- polysaccharides. Cellulolytic enzymes are another class of tergents. In addition to raising the level of cleaning, they have hydrolases that provide fabric care through selective reac- also provided environmental benefits by reducing energy con- sumption through shorter washing times, lower washing tem- tions not previously possible on fabrics. Research is cur- peratures, and reduced water consumption. Today proteases are rently underway into the possibility of using redox en- joined by lipases and amylases in improving detergent efficacy zymes—oxidases or peroxidases—for bleaching colored especially for household laundering at lower temperatures and, components (2). in industrial cleaning operations, at lower pH levels. Cellulases To support the 18–19-million -ton global annual market contribute to overall fabric care by rejuvenating or maintaining for laundry and dishwashing detergents (3), the world- the new appearance of washed garments. Enzymes are pro- wide consumption of detergent enzymes amounted to duced by fermentation technologies that utilize renewable re- ca.
    [Show full text]
  • Istanbul Technical University Institute of Science And
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE ISTANBUL TECHNICAL UNIVERSITY INSTITUTE OF SCIENCE AND TECHNOLOGY PARTIAL PURIFICATION AND CHARACTERIZATION OF ALKALINE PROTEASES FROM ISOLATED BACILLUS STRAINS M.Sc. Thesis by M.Hale Öztürk Department: Advanced Technologies Programme: Molecular Biology - Genetics & Biotechnology JANUARY 2005 ISTANBUL TECHNICAL UNIVERSITY INSTITUTE OF SCIENCE AND TECHNOLOGY PARTIAL PURIFICATION AND CHARACTERIZATION OF ALKALINE PROTEASES FROM ISOLATED BACILLUS STRAINS M.Sc. Thesis by M.Hale Öztürk (707021002) Date of submission : 27 December 2004 Date of defence examination : 25 January 2005 Supervisors : Assist. Prof. Dr. Hakan BERMEK Assoc. Prof. Dr. Yüksel AVCIBAŞI GÜVENİLİR Members of the Examining Committee : Prof. Dr. Bülent GÜRLER (İ.Ü.) Assist. Prof. Dr. Ayten YAZGAN KARATAŞ (İ.T.Ü.) Assist. Prof. Dr. Nevin GÜL KARAGÜLER (İ.T.Ü.) JANUARY 2005 İSTANBUL TEKNİK ÜNİVERSİTESİ FEN BİLİMLERİ ENSTİTÜSÜ İZOLE EDİLEN BACILLUS TÜRLERİNDEN ALKALİN PROTEAZ ENZİMİNİN KISMİ SAFLAŞTIRILMASI VE KARAKTERİZASYONU YÜKSEK LİSANS TEZİ Kim.Müh. M.Hale Öztürk (707021002) Tezin Enstitüye Verildiği Tarih : 27 Aralık 2004 Tezin Savunulduğu Tarih : 25 Ocak 2005 Tez Danışmanları : Yrd. Doç. Dr. Hakan BERMEK Doç. Dr. Yüksel AVCIBAŞI GÜVENİLİR Diğer Jüri Üyeleri : Prof. Dr. Bülent GÜRLER (İ.Ü.) Yrd. Doç. Dr. Ayten YAZGAN KARATAŞ (İ.T.Ü.) Yrd. Doç. Dr. Nevin GÜL KARAGÜLER (İ.T.Ü.) OCAK 2005 ACKNOWLEDGEMENTS I would like to thank to Assoc. Prof. Yüksel Avcıbaşı Güvenilir for being not only my supervisor but also for supporting, encouraging me in every step of this work. I would like to thank to my supervisor Assist. Prof. Hakan Bermek for his assistance during my thesis.
    [Show full text]
  • Stabilization of a Lipolytic Enzyme for Commercial Application
    Article Stabilization of a Lipolytic Enzyme for Commercial Application Simone Antonio De Rose 1, Halina Novak 1,†, Andrew Dowd 2,†, Sukriti Singh 2, Dietmar Andreas Lang 2 and Jennifer Littlechild 1,* 1 Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK; [email protected] (S.A.D.R.); [email protected] (H.N.) 2 Unilever R&D, HomeCare Discover, Disruptive Biotechnology, Quarry Road East, Bebington CH63 3JW, UK; [email protected] (A.D.); [email protected] (S.S.); [email protected] (D.A.L.) * Correspondence: [email protected]; Tel.: +44-0-1392-723468 † At the time of project execution. Academic Editor: David D. Boehr Received: 26 January 2017; Accepted: 10 March 2017; Published: 21 March 2017 Abstract: Thermomyces lanouginosa lipase has been used to develop improved methods for carrier- free immobilization, the Cross-Linked Enzyme Aggregates (CLEAs), for its application in detergent products. An activator step has been introduced to the CLEAs preparation process with the addition of Tween 80 as activator molecule, in order to obtain a higher number of the individual lipase molecules in the ”open lid” conformation prior to the cross-linking step. A terminator step has been introduced to quench the cross-linking reaction at an optimal time by treatment with an amine buffer in order to obtain smaller and more homogenous cross-linked particles. This improved immobilization method has been compared to a commercially available enzyme and has been shown to be made up of smaller and more homogenous particles with an average diameter of 1.85 ± 0.28 μm which are 129.7% more active than the free enzyme.
    [Show full text]
  • WO 2014/100018 Al 26 June 2014 (26.06.2014) W P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2014/100018 Al 26 June 2014 (26.06.2014) W P O P C T (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every C12N 9/24 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, (21) International Application Number: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, PCT/US2013/075829 DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, 17 December 2013 (17. 12.2013) KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (25) Filing Language: English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, (26) Publication Language: English SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (30) Priority Data: ZW. 61/739,267 19 December 2012 (19. 12.2012) US (84) Designated States (unless otherwise indicated, for every (71) Applicant: DANISCO US INC. [US/US]; 925 Page Mill kind of regional protection available): ARIPO (BW, GH, Road, Palo Alto, California 94304 (US). GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (72) Inventors: BARNETT, Christopher C ; Danisco US Inc., TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, 925 Page Mill Road, Palo Alto, California 94304 (US).
    [Show full text]
  • Preliminary Screening and Characterization of Novel Proteolytic Enzymes Produced by Extremophilic Bacteria Isolated from Tunisian and Algerian Biotopes
    Submitted on: 15/03/2021 Revue Revised form accepted on: 14/06/2021 Nature et Technologie Corresponding author: [email protected] http://www.univ-chlef.dz/revuenatec ISSN : 1112-9778 – EISSN : 2437-0312 Preliminary screening and characterization of novel proteolytic enzymes produced by extremophilic bacteria isolated from Tunisian and Algerian biotopes Sondes MECHRI a, Khelifa BOUACEM b,c, Fawzi ALLALAb, Marwa KHALED a, Amel b b a, BOUANANE-DARENFED , Hocine HACÈNE , Bassem JAOUADI * a Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Center of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax 3018, Tunisia b Laboratory of Cellular and Molecular Biology (LCMB), Microbiology Team, Faculty of Biological Sciences (FSB), University of Sciences and Technology Houari Boumediene (USTHB), P.O. Box 32, El Alia, Bab Ezzouar, 16111 Algiers, Algeria c Department of Biochemistry & Microbiology, Faculty of Biological and Agricultural Sciences (FBAS), University Mouloud Mammeri of Tizi-Ouzou (UMMTO), P.O. Box 17, Tizi-Ouzou 15000, Algeria Abstract The current paper reports on the production and characterization of extracellular thermostable proteases produced from thermophilic bacteria namely Aeribacillus pallidus VP3, Anoxybacillus kamchatkensis M1V, Virgibacillus natechei FarDT, and Melghiribacillus thermohalophilus Nari2AT strains isolated from different extremophlic biotopes in Tunisia and Algeria. The key challenge of the use of the different proteases in industrial applications is their efficiency under unconventional conditions. An optimization via one-factor-at-a-time (OFAT) methodology has been used to obtain 3,000 U.mL-1; 4,600 U.mL-1; 15,800 U.mL-1; and 16,000 U.mL-1 of proteases activity from VP3, M1V, FarDT, and Nari2AT strains, respectively.
    [Show full text]
  • Effect of Selected Enzymes on Performance of Liquid Laundry Detergents
    EFFECT OF SELECTED ENZYMES ON PERFORMANCE OF LIQUID LAUNDRY DETERGENTS Anita Bocho-Janiszewska University of Technology and Humanities in Radom, Faculty of Materials Science and Design, Department of Chemistry, Corresponding address: Chrobrego Str. 27, 26-600 Radom, Poland, [email protected] Abstract : The article examines the effect of type of selected enzymes on the performance of liquid laundry detergents. Enzymes are the catalysts of biological processes. Like any other catalyst, an enzyme brings the reaction catalyzed to its equilibrium position more quickly than it would occur otherwise. The most widely used detergent enzymes are hydrolases, which remove soils consisting of proteins, lipids, and poly-saccharides. Soil and stain components with good water solubility are easily removed during the cleaning process. Most other stains are partially removed by the surfactant system of a detergent, although the result is often unsatisfactory. In most cases a suitable detergent enzyme aids the removal of soils and stains. Whereas the detergent components have a purely physicochemical action, enzymes act by degrading the dirt into smaller and more soluble fragments. In the research samples of liquid laundry detergent containing selected hydrolases (lipase, amylase and protease) were prepared. Tests of the performance of liquid laundry detergents: viscosity, foaming properties and washing properties were conducted. Studies were carried out at three differe nt temperatures: 20, 30 and 40° C. For the sake of comparison, the same tests were also performed for a commercially available product. The addition of the enzyme does not affect the viscosity and foaming ability of the liquid laundry detergent. The ability to remove stains by the liquids containing enzymes was high even at a lower temperature.
    [Show full text]