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نویسندگان: 

SAYYAR KAVARDI S.S. | ALEMZADEH I. | KAZEMI A.

اطلاعات دوره: 
  • سال: 

    2012
  • دوره: 

    25
  • شماره: 

    1 (TRANSACTIONS C: ASPECTS)
  • صفحات: 

    1-9
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    428
  • دانلود: 

    0
چکیده: 

Pseudomonas aeruginosa BBRC-10036 was used for lipase production. The organism secreted the enzyme extracellulary. In order to purify the enzyme, precipitation was carried out first, and then this lipase was purified by Ion Exchange Chromatography leading to 2.3-fold purification and 11.47% recovery. Lipase from P.aeruginosa was entrapped into Ca-alginate gel beads and effect of independent variables such as alginate concentration (%w/v), CaCl2 concentration (M) and enzyme load (%v/v) on immobilization yield and activity of immobilized enzyme were investigated. Media optimization for immobilization of lipase was carried out by Response Surface Methodology. The optimum conditions were: sodium alginate concentration 2.5% (w/v), calcium chloride concentration 2.5 (M) and enzyme load 50% (v/v). Under these conditions, the highest immobilization yield and the optimum activity of immobilized enzyme obtained were 93.65% and 2.64 unit/g (IME), respectively.

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نشریه: 

زیست فناوری

اطلاعات دوره: 
  • سال: 

    1398
  • دوره: 

    10
  • شماره: 

    3
  • صفحات: 

    351-361
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    516
  • دانلود: 

    111
چکیده: 

در این تحقیق تفکیک انانتیومرهای ایبوپروفن راسمیک توسط آنزیم لیپاز تثبیت شده Rhizomucor miehei lipase (RML) روی مشتقات سیلیکا و نانوذره متخلخل سیلیکا SBA-15 مورد مطالعه قرار گرفت. به این منظور و برای بهره مندی از مزایای دو روش جذب هیدروفوب و اتصال کوالانسی، تثبیت آنزیم RML روی بسترهای حاوی دو گروه عاملی متفاوت به صورت همزمان صورت پذیرفت. اصلاح شیمیایی بسترهای سیلیکا و نانوذرات حفره دار سیلیکاتی توسط دو عامل با نسبت های مختلف انجام شد؛ عامل اکتیل تری اتوکسی سیلان (OTES) به عنوان عامل هیدروفوب کننده و 3-گلایوکسی پروپیل-تری متوکسی سیلان (GPTMS) به منظور اتصال کووالانسی آنزیم RML انتخاب شد. نتایج به دست آمده نشان می دهد، مشتقات به دست آمده از آنزیم RML تثبیت شده روی بسترهای حاوی گروه عامل اکتیل، فعالیت ویژه ای در حدود 1/5 تا 2 برابر فعالیت ویژه آنزیم آزاد دارند. همچنین با افزایش تعداد گروه های اپوکسی، فعالیت مضاعف و میزان رهایش آنزیم کاهش یافت. مناسب ترین بستر، با توجه به بررسی فعالیت ویژه پس از تثبیت و رهایش آنزیم RML، مربوط به مشتق به دست آمده از بستری بود که گروه های عاملی اپوکسی و اکتیل را با نسبت یک به یک دارد. مشتق حاضر و همچنین مشتقات به دست آمده با جذب صرفاً هیدروفوب برای سنتز استرهای فرم S-پروفن مورد استفاده قرار گرفت. استریفیکاسیون در شرایط دمایی مختلف و مقادیر متفاوت بیوکاتالیست انجام شد. نتایج حاصل از این تحقیق نشان داد بهترین میزان تفکیک انانتیومر S-ایبوپروفن مربوط به بسترهای سیلیکا اکتیل اپوکسی 1/1 و SBA اکتیل-اپوکسی 1/1 در دمای محیط بود.

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نویسنده: 

NASIRIRAD SOLMAZ | AGHAEI HAMIDREZA

اطلاعات دوره: 
  • سال: 

    2014
  • دوره: 

    17
تعامل: 
  • بازدید: 

    162
  • دانلود: 

    0
چکیده: 

BACKGROUND: LIPASE (TRIACYLGLYCEROL HYDROLASE, EC 3.1.1.3) IS ONE OF THE MOST EXTENSIVELY USED ENZYMES THAT CATALYZED THE HYDROLYSIS OF TRIACYL-GLYCEROL TO GLYCEROL AND FATTY ACIDS IN OIL–WATER INTERFACE SYSTEMS [1, 2]. THEREFORE, IT WAS NECESSARY TO IMPROVE THE IMMOBILIZATION STABILITY [3]. IN THE PRESENT STUDIED FOCUSED TOWARDS THE IMMOBILIZATION AND FURTHER TO BE EMPLOYED FOR OLIVE OIL HYDROLYSIS.METHODS: THE ACTIVATION OF HYDROXYL GROUPS OF CLOISITE WAS ACHIEVED BY REACTION WITH TSCL. AFTERWARD; TOSYLATED CLOISITE WAS MODIFIED WITH 4-HYDROXY BENZALDEHYDE. FOR IMMOBILIZATION OF LIPASE, ACTIVATED CLOISITE CONTINUOUSLY STIRRING THE REACTION MEDIUM AND WAS EMPLOYED FOR OLIVE OIL HYDROLYSIS. THE HYDROLYSIS ACTIVITY FOR OLIVE OIL WAS MEASURED BY THE TITRIMETRIC METHOD WITH FEW MODIFICATIONS.RESULTS: IN THIS STUDY THE OPTIMUM PH FOR LIPASE ACTIVITY VARIES, WITH THE ENZYME SPECIES. IN OUR STUDY PH OPTIMUM ACTIVITY OF IMMOBILIZED LIPASES WAS 73%. BECAUSE ENZYMATIC ACTIVITY IS OBVIOUSLY TEMPERATURE DEPENDENT, THE CATALYTIC ACTIVITY OF IMMOBILIZED LIPASE WAS TESTED AT DIFFERENT TEMPERATURES (40-80OC), A MAXIMUM OF ACTIVITY WAS RECORDED AT 55OC.CONCLUSION: IN THE PRESENT STUDY, TOSYLATED CLOISITE WAS PREPARED BY MODIFICATION WITH 4-HYDROXY BENZALDEHYDE.

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اطلاعات دوره: 
  • سال: 

    2022
  • دوره: 

    26
  • شماره: 

    2
  • صفحات: 

    153-159
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    73
  • دانلود: 

    0
چکیده: 

Background: Lipase enzymes are of great importance in various industries. Currently, extensive efforts have been focused on exploring new lipase producer microorganism as well as genetic and protein engineering of available lipases to improve their functional features. Methods: For screening lipase-producing lactobacilli, isolated strains were inoculated onto tributyrin agar plates. Molecular identification of lipaseproducing Lactobacilli was performed by sequencing the 16Sr DNA gene, and a phylogenetic tree was constructed. The LAF_RS05195 gene, encoding lipase protein in L. fermentum isolates, was identified using specific primers, amplified by PCR (918 bp) and cloned into the pET28a (+) vector. The recombinant proteins were expressed 2, 4, 6, and 12 hours after induction with IPTG and assessed using the SDS-PAGE. Enzymatic activity of the purified recombinant protein was measured at 410 nm in the presence of ρ NPA and ρ-NPP. Results: Among five identified native lipase-producing isolates, one isolate showed 98% similarity with Enterococcus species. The other four isolates indicated 98% similarity to L. fermentum. After purification steps with NiNTA column, a single protein band of about 34 kDa was detected on SDS-PAGE gel. The enzymatic activity of purified recombinant protein alongside ρ-NPA and ρ-NPP was measured to be 0. 6 U/ml and 0. 2 U/ml, respectively. Conclusion: In the present research, a novel lipase/esterase from L. fermentum was cloned and expressed. The novel lipase/esterase has the merit to be further studied due to its substrate specificity.

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اطلاعات دوره: 
  • سال: 

    2020
  • دوره: 

    14
  • شماره: 

    6
  • صفحات: 

    23-27
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    173
  • دانلود: 

    0
چکیده: 

Background and objectives: Industrial wastewater is worldwide health concern. Microorganisms present in the environment have an important role in the biodegradation of lipids, fats and proteins from wastewater. In this regard, microbial lipases and proteases are interesting research targets because of high stability, broad substrate specificity, high yields and availability. In this study, we analyze sequences encoding lipase of Pseudomonas putida and subtilisin of Bacillus subtilis for generation of a new recombinant protein for degradation of environmental contaminations caused by lipids and proteins. Methods: In this study, sequences of the genes encoding lipase and subtilisin were obtained from GenBank. To predict the 3D structure of the protein, modeling was carried out. The prediction of secondary structure, tertiary structure and solvent accessibility was carried using bioinformatics tools including I-TASSER, GoR4 and ExPasy. Results: The lipase-subtilisin fusion protein was wellcharacterized by bioinformatical studies with appropriate spatial and secondary structures. The protein had appropriate hydrophilicity, biological half-life and thermal and acidic stability. The codon optimization was performed appropriately. Conclusion: Overall, the bioinformatical analysis of the designed protein showed that the recombinant lipase-subtilisin protein has a stable structure both in vitro and in vivo, a negative normalized B-factor and lipolytic and proteolytic activities, which makes it suitable for treatment of lipid and protein contaminations.

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نویسنده: 

AGHAEI HAMIDREZA | Mokhtari Azam

اطلاعات دوره: 
  • سال: 

    2014
  • دوره: 

    21
تعامل: 
  • بازدید: 

    157
  • دانلود: 

    0
کلیدواژه: 
چکیده: 

ENZYMECATALYZED POLYMERIZATION REACTIONS IN ORGANIC SOLVENTS HAS BEEN IMPORTANT IN ORGANIC SYNTHESIS AND HAS BEEN PROVEN TO BE A NEW METHODOLOGY IN POLYMER SYNTHESIS [1]. CHARACTERISTIC FEATURES OF ENZYME CATALYSIS AFFORDED NOVEL POLYMERIZATION REACTIONS TO PRODUCE POLYMERS, WHICH ARE OFTEN DIFFICULT TO BE SYNTHESIZED BY CONVENTIONAL POLYMERIZATIONS. ...

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نویسندگان: 

نشریه: 

SCIENTIFIC WORLD JOURNAL

اطلاعات دوره: 
  • سال: 

    2022
  • دوره: 

    2022
  • شماره: 

    -
  • صفحات: 

    0-0
تعامل: 
  • استنادات: 

    1
  • بازدید: 

    7
  • دانلود: 

    0
کلیدواژه: 
چکیده: 

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اطلاعات دوره: 
  • سال: 

    2014
  • دوره: 

    17
تعامل: 
  • بازدید: 

    134
  • دانلود: 

    0
چکیده: 

BACKGROUND: NOWADAYS, VEGETABLE USED OILS ARE A POTENTIAL RENEWABLE SOURCE FOR THE PRODUCTION OF AN ALTERNATIVE FOR PETROLEUM BASED DIESEL FUEL DUE TO THE DIMINISHING PETROLEUM RESERVES AND THE ENVIRONMENTAL CONSEQUENCES OF EXHAUST GASES FROM DIESEL ENGINES. THE BIODIESEL PRODUCTION FROM VEGETABLE OILS INVOLVES THE TRANS ESTERIFICATION OF VEGETABLE OILS USING A SHORT CHAIN ALCOHOL IN THE PRESENCE OF A SUITABLE CATALYST OBTAINING A FUEL QUITE SIMILAR TO CONVENTIONAL DIESEL FUEL IN ITS MAIN CHARACTERISTICS [1]. ENZYMATIC BIODIESEL PRODUCTION FROM RAW VEGETABLE OILS HAS BEEN EXTENSIVELY STUDIED FOR MANY AUTHORS IN THE LAST YEARS [2-4]. IN THIS STUDY, OLIVE OIL WAS USED AS FOR ENZYMATIC BIODIESEL PRODUCTION. THE PURPOSE OF THIS WORK IS TO ANALYZE THE INFLUENCE OF OPERATING PARAMETERS, SUCH AS METHANOL TO OIL MOLAR RATIO, DOSAGE OF ENZYME, REACTION TIME AND ENZYME REUSE ON TRANS ESTERIFICATION PROCESS.METHODS: THE ACTIVATION OF HYDROXYL GROUPS OF CLOISITE WAS ACHIEVED BY REACTION WITH P-TOLUENESULFONYL CHLORIDE. FOR PREPARATION OF AMINATED CLOISITE, TOSYLATED CLOISITE WAS DISPERSED IN A FLASK CONTAINING HEXAMETHYLENE DIAMINE. THE ACTIVATION OF AMINO GROUPS OF THE ACTIVATED CLOISITE WAS ACHIEVED BY REACTION WITH EPICHLOROHYDRIN. FOR IMMOBILIZATION OF LIPASE, ACTIVATED CLOISITE WERE EQUILIBRATED IN PHOSPHATE BUFFER AND TRANSFERRED TO THE SAME FRESH MEDIUM CONTAINING LIPASE. THE ENZYMATIC TRANS ESTERIFICATION REACTIONS WERE CARRIED OUT IN A TEST TUBE CONTAINING 0.1 ML OF OLIVE OIL, 500 MG OF IMMOBILIZED LIPASE AND METHANOL. THE MOLAR AMOUNT OF THE OIL WAS CALCULATED FROM THE ACID VALUE. THE REACTION WAS CARRIED OUT IN AN INCUBATOR AT 50OC DURING 4 H WITH CONSTANT STIRRING.RESULTS: AT THIS STUDY, EFFECTS OF TEMPERATURE, REACTION TIME, MOLAR RATIO (METHANOL TO OIL) AND TYPE OF SOLVENT ARE INVESTIGATED. REMARKABLY, THE OPTIMUM REACTION CONDITIONS ARE METHANOL TO OIL MOLAR RATIO OF 10:1, REACTION PERIOD OF 4 H AT 50OC IN N-HEXANE.CONCLUSION: IMMOBILIZED LIPASE CATALYZED BIODIESEL PRODUCTION ALLOWS THE USE OF MILD AND MORE ENVIRONMENTALLY FRIENDLY REACTION CONDITIONS. THE RESULTS INDICATED THAT THROUGH THE OPTIMIZATION OF REACTION CONDITIONS, BIODIESEL WAS OBTAINED IN ALMOST 60% AND THERE WAS NO OBVIOUS LOSS IN THE YIELD OF BIODIESEL AFTER BEING CONSECUTIVELY USED FOR SIX CYCLES IN THE TRANS ESTERIFICATION REACTIONS USING IMMOBILIZED LIPASE.

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اطلاعات دوره: 
  • سال: 

    1395
  • دوره: 

    12
  • شماره: 

    49
  • صفحات: 

    167-176
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    2017
  • دانلود: 

    683
چکیده: 

هدف اصلی از اجرای این پژوهش، بررسی امکان استفاده از آنزیم لیپاز به عنوان بیوامولسیفایر برای تهیه نان باگت بود. لیپاز در سه سطح 10، 30 و 50 ppm مورد استفاده قرار گرفت. در این تحقیق ویژگی های شیمیایی آرد تعیین گردید و تاثیر استفاده از آنزیم در سه سطح به طور مجزا بر ویژگی های حجم، رطوبت، بیاتی و رنگ ارزیابی شد و ویژگی های حسی توسط 10 ارزیاب آموزش دیده مورد بررسی قرار گرفتند. نتایج نشان داد که در ارزیابی حسی تفاوت معنی داری بین تیمارها از نظر صفت عطر و بو، حجم، مزه، رنگ پوسته، تناسب شکل، ترک و پارگی و مجموع امتیازات ویژگیهای ظاهری نسبت به یکدیگر و تیمار شاهد وجود نداشت (p>0.05). نان های تهیه شده در مقادیر 10 و 30 پی پی ام آنزیم لیپاز امتیاز بیشتری در صفات ویژگی های بافت داخلی، ویژگی های پوسته، بهبود قابلیت جویدن، حفره بندی مناسب بافت نسبت به تیمار شاهد نشان دادند ولی در این بین استفاده از 10 پی پی ام لیپاز بیشترین امتیاز را در پذیرش کلی صفات حسی نشان داد. بنا به نتایج حاصل از آزمونهای بافت سنجی مشخص گردید لیپاز در دو غلظت 10 و 30 پی پی ام از نظر کاهش سفتی مطلوب تر و نان حاصل از 30 پی پی ام لیپاز دارای حداکثر حجم نسبت به سایر مقادیر می باشد. نتایج آزمون رنگ سنجی نیز نشانگر این مطلب بود که آنزیم لیپاز در میزان 10 پی پی ام بهترین رنگ مغز نان و در غلظت 30 پی پی ام بهترین رنگ پوسته را نسبت به سایر تیمارها ایجاد می کند و حداکثر رطوبت مشاهده شده بین تیمارها مربوط به نان حاصل از 30 پی پی ام آنزیم لیپاز بود که نسبت به سایر تیمارها اختلاف معنی دار بود (p<0.05).

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اطلاعات دوره: 
  • سال: 

    2015
  • دوره: 

    16
تعامل: 
  • بازدید: 

    155
  • دانلود: 

    0
چکیده: 

BACKGROUND AND AIM: THE PURPOSE OF THIS STUDY IS PREPARATION INDUSTRIAL ENZYME LIPASE FROM INDUSTRIAL MICROBIOLOGY.METHODS: BECAUSE DISCUSSED IN THE REVIEW OF THE ENVIRONMENT CULTURE FOR LIPASE ENZYMES WAS INVESTIGATED. DESIGN ENVIRONMENT CULTURE IN THE LABORATORY IS OFTEN COSTLY AND TIME CONSUMING PROCESS WHICH REQUIRES MULTIPLE EXPERIMENTS IS ALSO GENERAL METHODS FOR DESIGNING AN OPTIMAL ENVIRONMENT CULTURE, THE CONCENTRATION OF THE INGREDIENTS OF INDIVIDUALLY OR AT THE SAME TIME BY A FACTOR THIS METHOD CAN ONLY BE GOOD CONCENTRATION FOR EACH FACTOR SEPARATELY ACQUIRED….

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