کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8327102 | 1540197 | 2018 | 37 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Production, purification and characterization of raw starch hydrolyzing thermostable acidic α-amylase from hot springs, India
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کلمات کلیدی
SECDTTGeobacillusPMSFα-Amylase - α-آمیلازβ-mercaptoethanol - β-merkaptoethanolβ-Me - β-منEDTA - اتیلن دی آمین تترا استیک اسید Ethylenediaminetetraacetic acid - اتیلینیدامین تتراستیک اسیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتSize-exclusion chromatography - اندازه گیری کروماتوگرافی حذف شدهThermostability - ترموستاتاdithiothreitol - دیتیوتریتولphenyl methyl sulfonyl fluoride - فنیل متیل سولفونیل فلورایدSEM - مدل معادلات ساختاری / میکروسکوپ الکترونی روبشیscanning electron microscope - میکروسکوپ الکترونی اسکنRaw starch - نشاسته خام
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Alpha-amylase is an important hydrolytic enzyme used for various industrial processes. In the present study, Geobacillus bacterium (K1C), producing a thermostable α-amylase was isolated from Manikaran hot springs, India. We have purified and characterized the biochemical properties of α-amylase. The optimum temperature and pH for α-amylase activity was 80â¯Â°C and pHâ¯6.0 respectively. The far-UV CD spectra of the enzyme indicated the presence of random coil conformation and showed an intermediate phase during temperature-induced unfolding. In the presence of substrate, thermostability of the α-amylase was increased as 50% initial activity was retained at 70â¯Â°C for 6â¯h and at 80â¯Â°C for 2â¯h. Moreover, the enzyme also showed remarkable pH stability as 90% of the initial activity was retained even after 48â¯h of incubation at pHâ¯5.0, 6.0 and 7.0. Interestingly, amylase activity of the purified enzyme was Ca2+independent, whereas the complete inhibition of activity was observed in the presence of Cu2+, Pb2+, and Hg2+. The purified α-amylase was stable in the presence of detergents, organic solvents and Proteinase K. Furthermore, it exhibited the ability to hydrolyze raw starches (e.g. rice, wheat, corn, potato) efficiently; thus this enzyme has the potential to be used for industrial applications.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 117, 1 October 2018, Pages 831-839
Journal: International Journal of Biological Macromolecules - Volume 117, 1 October 2018, Pages 831-839
نویسندگان
Sarabjeet Kour Sudan, Narender Kumar, Ishwinder Kaur, Girish Sahni,