Action of Millimeter-range Electromagnetic Radiation on Polypeptide Spectrum of Amylolytic Preparations from Aspergillus Niger 33-19 CNMN FD 02A Strain
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DESYATNIK, A., BIVOL, Cezara, STRATAN-BINZARI, Maria, TIURINA, Janeta, CLAPCO, Steliana, REVA, Veaceslav, LABLYUK, S.. Action of Millimeter-range Electromagnetic Radiation on Polypeptide Spectrum of Amylolytic Preparations from Aspergillus Niger 33-19 CNMN FD 02A Strain. In: Электронная обработка материалов, 2014, nr. 1(50), pp. 72-77. ISSN 0013-5739.
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Электронная обработка материалов
Numărul 1(50) / 2014 / ISSN 0013-5739 /ISSNe 2345-1718

Action of Millimeter-range Electromagnetic Radiation on Polypeptide Spectrum of Amylolytic Preparations from Aspergillus Niger 33-19 CNMN FD 02A Strain
CZU: 621.372:577.151

Pag. 72-77

Desyatnik A.1, Bivol Cezara1, Stratan-Binzari Maria1, Tiurina Janeta1, Clapco Steliana1, Reva Veaceslav2, Lablyuk S.1
 
1 Institute of Microbiology and Biotechnology of the ASM,
2 Moldova State University
 
Disponibil în IBN: 18 martie 2017


Rezumat

Micromycete Aspergillus niger 33-19 CNMN FD 02A standard cultivated and exposed to λ = 7.1 millimeter waves radiation has been used to obtain two enzyme preparations with the 10x degree of purity, with a 29.9% difference of the α-amylase activity in irradiated preparation but with a similar specific activity of protein of 138.3 U/mg and 141.0 U/mg. The α-amylase purification through gel filtration and ion exchange chromatography has resulted in the increase of 8.9 times of the specific activity for the control and of 8.2 times for the irradiated samples, with the yields of 25% and 17%, respectively. The SDS-PAGE of proteins isolated from initial preparations indicates the expression of new polypeptide of 45 kDa in the irradiated samples. Polypeptide spectrum of α-amylase from both preparations, purified through ion chromatography, shows two unchanged polypeptide bands of 66 and 40.5 kDa, identified as α-amylase isomorphs.

Из мицелиального гриба Aspergillus niger 33-19 CNMN FD 02A, культивируемого в стандартных условиях и после облучения миллиметровыми волнами λ = 7,1, были получены два ферментных препарата со степенью очистки Г10x, отличающихся по уровню амилолитической активности (на 29,9% выше в препарате, подвергнутом облучению), но с идентичной специфической активностью в 138,3 ед/мг и 141,0 ед/мг белка. Очистка α-амилазы методами гель-фильтрации и ионообменной хроматографии привела к увеличению специфической активности в 8,9 раз в контрольном и в 8,2 раза в облученном препаратах, с 25% и 17% выходом, соответственно. SDS-ПААГ белков, выделенных из начальных препаратов, показала появление нового полипептида с молекулярной массой 45 kDa в образце, подвергнутом облучению. Полипептидный спектр очищенной α-амилазы обоих препаратов после ионной хроматографии представляет 2 неизменныe полипептидныe полосы с молекулярной массой 66 и 40,5 kDa, определенных как изоформы α-амилазы.

Cuvinte-cheie
millimeter-range electromagnetic radiation, α-amylase purification,

Fungi, Aspergillus niger

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