Rzaeva O. alpha-L-Rhamnosidase of Penicillium commune 266.

Українська версія

Thesis for the degree of Candidate of Sciences (CSc)

State registration number

0407U003979

Thesis Registration Form

0407U003979.pdf

Applicant for

Specialization

  • 03.00.07 - Мікробіологія

17-10-2007

Specialized Academic Board

Д 26.233.01

D.K. Zabolotny Institute of Microbiology and Virology of the NASU

Essay

The screening among 692 cultures of fungi and bacteria permit to select strain P. commune 266 producer of alpha-L-rhamnosidase. The scheme of enzyme purification have been developed. Two preparations with alpha-L-rhamnosidase activity were isolated from culture liquid and purified about 207 and 67-times, activity of enzyme preparations 1 and 2 were 157 and 51 U/mg protein, respectively. The physico-chemical, catalytic properties and specify of action of enzymes has been studied. Enzyme preparations included high contents of basic and hydrophobic aminoacids and 2% of carbohydrate component. Enzyme 2 was found to exhibit strict specificity towards the glycon at the same time enzyme 1 exerted wide specificity. alpha-L-Rhamnosidase 1 and 2 active centers appears to contain the carboxyl group of C-terminal aminoacid and imidazole histidine group. Sulfhydrylic groups are not involved in the catalysis. However, it's possible they may play essential role in supporting the active conformation of the protein molecule.

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Files

aref.doc

aref.doc

дисер-жовтень--Вступ.doc

дисер-жовтень--ЗАКЛЮЧЕННЯ.doc

дисер-жовтень--Література ст.doc

дисер-жовтень--Розділ 1.doc

дисер-жовтень--Розділ 3.doc

дисер-жовтень--Розділ 4.doc

дисер-жовтень--Розділ 4.doc

дисер-жовтень--розділ 10.doc

дисер-жовтень--розділ 2.doc

дисер-жовтень--розділ 5.doc

дисер-жовтень--розділ 6.doc

дисер-жовтень--розділ 7.doc

дисер-жовтень--розділ 8.doc

дисер-жовтень--розділ 9.doc

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