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اطلاعات دوره: 
  • سال: 

    2021
  • دوره: 

    5
  • شماره: 

    9
  • صفحات: 

    0-0
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    73
  • دانلود: 

    0
چکیده: 

Inulinases are a class of enzymes that are widely used to produce fructose syrup. Due to the importance of this group enzyme in the production of fructose and high fructose syrup, developed countries continue to research in this field. The most important source of inulinase production is microorganisms. In this article, firstly, the structure, types, and applications of inulinases are mentioned and then its global market is discussed based on various criteria. Further, solid-state fermentation is overviewed as a suitable production system for industrial production of this enzyme and finally, the production and refining stages as well as challenges in their production are addressed and solutions to overcome these problems are proposed.

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نویسندگان: 

ALLAIS J.J. | KAMMOUN S. | BLANC P.

اطلاعات دوره: 
  • سال: 

    1986
  • دوره: 

    52
  • شماره: 

    5
  • صفحات: 

    1086-1090
تعامل: 
  • استنادات: 

    1
  • بازدید: 

    184
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    0
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نویسندگان: 

ARAMOON KAMAL | AHANI AZARI ANIA

اطلاعات دوره: 
  • سال: 

    2014
  • دوره: 

    43
  • شماره: 

    SUPPLEMENT 2
  • صفحات: 

    128-128
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    285
  • دانلود: 

    0
چکیده: 

Background: Microbial Inulinases constitute an important class of enzymes that degrade inulin into fructooligosaccharides and high-fructose syrup which are widely used in pharmaceutical and food industry. These enzymes are produced by various microorganisms including bacterial strains, filamentous fungi and yeasts. The aim of this study was to isolate and screen wild-type inulinase producing bacterial strains from soil samples of Gorgan district, Golestan province.Methods: The soil samples were collected from different locations. The primary screening was performed based on hydrolytic zone on a inulin-based medium and Lugole`s iodine solution. Then morphological and biochemical characteristics of the isolated bacterial strains with inulinase activity were determined. Additionally, species-specific identification by 16S rDNA sequencing was performed on a few bacterial strains which had more inulinase activity.Results: Nineteen inulinase producing bacterial strains were isolated from the soil samples. Out of Nineteen strains, 4 bacterial strains with more inulinase activity were identified by 16S rDNA sequencing. The species-specific identification revealed these 4 isolates as Bacillu scereus strain BF15, Bacillus sp.AK16, Bacillus cereus strain LD22 and Enteroba ctercloacae P101. Bacillus pumilus strain PIA39 was found the nearest homolog to the Bacillus sp.AK16.Conclusion: We isolated and characterized inulinase producing bacterial strains from soil samples of Gorgan district. Most of them belonged to the Bacillus genus.

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نویسندگان: 

Surti Arjuman | Mhatre Sneha

اطلاعات دوره: 
  • سال: 

    2021
  • دوره: 

    8
  • شماره: 

    2
  • صفحات: 

    164-171
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    116
  • دانلود: 

    0
چکیده: 

Introduction: Inulinases are β-fructohydrolase enzymes that catalyze the hydrolysis of inulin. Recently, this enzyme has gained much importance mainly due to its ability to produce high-density fructose syrup using inulin as a raw material. In the current study, screening of inulinase-producing microorganisms was carried out from the rhizosphere soil of the Dahlia plant and rotten garlic samples. Materials and Methods: The inulinase activity was detected with the help of 3, 5-dinitrosalicylic acid (DNSA) and Seliwanoff’ s method, and the organism showing the highest potential was selected for further optimization studies. Results: The optimum culture conditions for inulinase production, by the test fungal culture, were observed when 5% inoculum was added to the minimal medium (pH 5. 5) containing 1% inulin/ costus root powder as a carbon source and 0. 15% NaNO3 / NH4 Cl as a nitrogen source, and incubated at 30° C for 48h under shaker conditions (200 rpm). Maximum enzyme activity was observed at pH level of 5 and temperature level of 45° C, with thermal stability noted between 35° C-55° C. The I/S value of the crude enzyme was calculated to be 0. 45 indicating true inulinase activity. It showed no significant inhibition in the presence of metal ions such as Zn 2+, Mg 2+, and Fe 3+. The Ca 2+ ions showed partial inhibition whereas Cu 2+ ions showed an enhancement in the enzyme activity. Conclusions: These factors may present the test fungal culture isolated in the present study to be a potential candidate for the production of thermotolerant and metal resistant inulinase enzyme in order to be used for various biotechnological processes.

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اطلاعات دوره: 
  • سال: 

    1397
  • دوره: 

    28
  • شماره: 

    1
  • صفحات: 

    15-25
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    258
  • دانلود: 

    103
چکیده: 

هدف این پژوهش بررسی ویژگی های ساختاری و عملکردی اندواینولیناز پس ازاصلاح با PLP برای آبکافت اینولین است. برای تعیین پایداری حرارتی، فعالیت باقیمانده هر دو آنزیم (اصلاح شده و شاهد) پس از 130 دقیقه انکوباسیون در دماهای مختلف در محدوده ° C25-65 اندازه گیری و برای تعیین پایداری زمانی، فعالیت هر دو آنزیم تا 6 روز بطور روزانه سنجیده شدند. جهت بررسی تغییرات ساختاری و نیز ارزیابی تغییرات ساختار دوم و سوم آنزیم اندواینولیناز، پس از اصلاح با PLP، از روش های طیف سنجی دورنگ نمایی دورانی، جذب سنجی در طول موج nm 280، فلوئورسانس برون زاد و درون زاد استفاده شد. کروماتوگرام محصولات حاصل از آبکافت اینولین توسط اندواینولیناز اصلاح شده با PLP یا اندواینولیناز دست نخورده با استفاده از HPLC بدست آمده و سپس پارامترهای کاتالیتیکی هر دو آنزیم محاسبه شدند. محتوای ساختار مارپیچ آلفا پس از اصلاح با PLP افزایش یافت، همچنین نتایج بررسی ساختار سوم شامل مطالعات طیف سنجی UV و نشر فلورسان، افزایش پایداری حرارتی اندواینولیناز بعد از اصلاح با PLP را تایید نمودند. نتایج آزمون های پایداری زمانی، حاکی از آن بود که افت فعالیت مشاهده شده در آنزیم اصلاح شده با PLP کمتر از آنزیم شاهد است. بهبود کارایی آنزیم اندواینولیناز جهت آبکافت اینولین پس از اصلاح با PLP توسط HPLC ثابت شد. پس از اصلاح آنزیم Vmax افزایش و Km کاهش یافت که نشانگر بهبود عملکرد آنزیم پس ازاصلاح با PLP است.

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اطلاعات دوره: 
  • سال: 

    1397
  • دوره: 

    12
  • شماره: 

    4
  • صفحات: 

    103-110
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    627
  • دانلود: 

    185
چکیده: 

سابقه و هدف: آنزیم اینولیناز آسپرژیلوس نایجر هیدرولیز کننده اینولین بوده و در تهیه شربت پرفروکتوز مورد استفاده قرار می گیرد. در این تحقیق، آنزیم اینولیناز از طریق ایجاد پیوند کووالانسی بر روی نانوذرات مغناطیسی هیدرولیزات گلوتنی گندم تثبیت گردید. این روش تثبیت، از نظر افزایش انتقال جرم بدلیل کاهش اندازه ذرات و افزایش سطح و در نتیجه بازدهی بیشتر فرآورده نهایی همچنین، بازیابی آنزیم تثبیت شده توسط میدان مغناطیسی از محیط واکنش و امکان استفاده مجدد از آنزیم دارای اهمیت است. مواد و روش ها: در ابتدا نانوپپتیدهای هیدرولیزات گلوتنی با روش حلال زدایی و نانوذرات مغناطیسی Fe3O4 به روش هم رسوبی تهیه شدند. سپس سطح نانوذرات مغناطیسی توسط نانوپپتیدهای تهیه شده پوشش داده شد و آنزیم اینولیناز از طریق پیوند کووالانسی بروی آن تثبیت گردید. ویژگی های ساختاری و عملکردی نانوذرات تهیه شده و آنزیم تثبیت شده با استفاده از روش های اسپکتروفتومتری در ناحیه UV/VIS و میکروسکوپ الکترونی روبشی گسیل میدانی تعیین گردید. یافته ها : مورفولوژی نانوذرات مغناطیسی بشکل کروی و نانوپپتیدهای گلوتنی بصورت کروی و رشته های کوتاه نشان داده شد. فاکتور های سینتیکی آنزیم تثبیت شده در مقایسه با آنزیم آزاد بهبود یافته و میزان بارگذاری آنزیم بر روی نانوپپتیدهای مغناطیسی حامل 74% محاسبه گردید. آنزیم اینولیناز تثبیت شده پس از 12 سیکل پی در پی آبکافت، 70% از فعالیت اولیه خود را حفظ نمود. نیمه عمر آنزیم تثبیت شده در دمای 60 درجه سانتی گراد در مقایسه با آنزیم آزاد حدود 1.5 برابر افزایش یافت. نتیجه گیری: استفاده از نانوپپتیدهای مغناطیسی هیدرولیزات گلوتنی گندم جهت تثبیت آنزیم اینولیناز، روشی کارآمد همراه با افزایش پایداری و بهبود عملکرد آنزیم به منظور تهیه شربت پرفروکتوز می باشد.

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اطلاعات دوره: 
  • سال: 

    2022
  • دوره: 

    12
  • شماره: 

    2
  • صفحات: 

    1729-1739
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    43
  • دانلود: 

    0
چکیده: 

Chicory is a rich plant source for the prebiotic inulin. The aim of this study was to evaluate the activity of purified inulinase enzyme from fungal strains on the inulin extracted from chicory. Inulin was extracted by soaking in water and precipitating in ethanol. Fungi were isolated from the soil around chicory root and screened for inulinase production along with fungal strains, Kluyveromyces marxianus PTCC 5006 and Aspergillus flavus PTCC 5304. The high inulinaseproducing fungal isolate was identified based on the sequencing of 18S rRNA gene. The enzyme was purified using ammonium sulfate-polyacrylamide and dialysis. The molecular weight of the protein was detected using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). One fungal isolate that showed high enzymatic activity (2233 U/ml) was obtained. This isolate was identified as the species Talaromyces moniliformis. Among the collection strains, Kluyveromyces marxianus had the highest inulinase production,while its inulinase activity was lower than that of Talaromyces moniliformis. The results from enzyme purification from Talaromyces moniliformis showed that the most specific enzyme activity (546. 6 U/mg) and the highest purification yield (62. 17%) were obtained by the precipitation in 55% ammonium sulfate. Dialysis of the protein resulted in the extraction of a protein with a reduced specific enzyme activity (188. 6 U/mg). The molecular weight of the purified protein was estimated at15 kDa. The fungal inulinase which purified from native resources in the present study can be used in food and pharmaceutical industries due to its high enzymatic activity.

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نویسندگان: 

اطلاعات دوره: 
  • سال: 

    2017
  • دوره: 

    98
  • شماره: 

    -
  • صفحات: 

    542-549
تعامل: 
  • استنادات: 

    1
  • بازدید: 

    67
  • دانلود: 

    0
کلیدواژه: 
چکیده: 

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اطلاعات دوره: 
  • سال: 

    2009
  • دوره: 

    17
  • شماره: 

    3
  • صفحات: 

    199-208
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    468
  • دانلود: 

    0
چکیده: 

Background: In the previous study it was shown that films prepared from inulin (In) in combination with Eudragit RS (ERS) and RL (ERL) were susceptible to inulinase. Purpose: The aim of this work was to assess the suitability of these combinations for colonic delivery of indomethacin.Methods: Indomethacin was loaded onto non-pareil seeds using fluidized bed apparatus to produce pellets with 20% w/w drug load. Drug loaded pellets were coated with In-ERS in the ratios of 20:80 and 30:70, or In-ERL in the ratio of 20:80 to different coating loads. The release of drug was examined in simulated gastric (for 2 hrs) and small intestine and in the presence of inulinase in simulated colonic medium (for 12 or 24 hrs). Results: The results of this study revealed that incorporation of inulin as a bacterially degradable polysaccharide into ERS or ERL could modulate drug release. Coating level up to 15% significantly affected drug release from In-ERL or In-ERS coated pellets. However further increase in coating load to 20% had no significant effect on drug release from In-ERL coated pellets (f1=9.39). Drug release from In-ERL coated pellets was faster and showed some pH dependency. Conclusions: Formulation coated with In-ERS (20:80) and coating level of 20% was considered more appropriate for colon delivery of indomethacin, as drug release was pH independent and formulation was resistant to drug release in the upper GI media for up to 7 hrs. This formulation was also susceptible to inulinase and released about 40% of indomethacin in the simulated colonic media.

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اطلاعات دوره: 
  • سال: 

    2011
  • دوره: 

    8
  • شماره: 

    4 (32)
  • صفحات: 

    705-714
تعامل: 
  • استنادات: 

    0
  • بازدید: 

    642
  • دانلود: 

    0
چکیده: 

Production of ten hydrolytic enzymes was qualitatively studied on the haloarchaeal strains isolated from Aran-Bidgol hypersaline lake in the central desert area of Iran. A total of 293 haloarchea strains were selected among 300 extremely halophilic isolated prokaryotes. Accordingly, 142, 141, 128, 64, 38, 16, 7, 3 and 1 archaeal isolates were able to produce DNase, amylase, lipase, inulinase, pullulanase, protease, cellulase, chitinase and xylanase, respectively. None was able to produce pectinase activity. Combined hydrolytic activity was also detected in many strains. A total of 0.3 % of the strains showed 6 hydrolytic activities, 0.3 % of the strains had 5 hydrolytic activities, 5.4 % of the strains presented 4 hydrolytic activities, 25 % of the strains presented 3 hydrolytic activities, 28 % of the strains presented 2 hydrolytic activities and 18 % of the strains presented 1 hydrolytic activity. According to their phenotypic characteristics and comparative partial 16 S rRNA sequence analysis, the halophilic strains were all identified as members of family Halobacteriaceae within 12 different taxa from the following genera: Halorubrum, Haloarcula, Natrinema, Halovivax and Natronomonas. Most enzymes production rate was observed in the genera Halorubrum, Haloarcula and Natrinema whereas; there was not any detectable amount of enzyme production in the genera Halovivax and Natronomonas. The most hydrolytic isolate with 6 combinatorial enzyme production belonged to the genus Natrinema. This investigation showed that the extreme halophilic archaea from Aran-Bidgol lake are a potential source of hydrolytic enzyme under stress conditions and may have possess commercial value.

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