Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Sanaa T. El-Sayed"'
Publikováno v:
Scientific Study & Research: Chemistry & Chemical Engineering, Biotechnology, Food Industry, Vol 21, Iss 2, Pp 141-154 (2020)
The objective of this study was to prepare bile acidsbinding and tyrosinase inhibitory peptides for industrial potential application. Proteins were extracted from Brassica olercea (cauliflower) midribs, Corchorus olitorius (corchorus) stems and Vic
Externí odkaz:
https://doaj.org/article/1b4385db4f214064bc365576d2a0bbea
Publikováno v:
Biocatalysis and Agricultural Biotechnology. 17:331-338
The present study was designed to prepare a novel tyrosinase inhibitory peptides from Solunum tuberosum (potato) peels (by-product of potato processing). Isolated protein was hydrolyzed by immobilized lettuce protease at pH 10 to produce a potato hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c326c6f82859aaa67e25843728db7716
https://doi.org/10.1016/j.bcab.2018.12.009
https://doi.org/10.1016/j.bcab.2018.12.009
Publikováno v:
Biocatalysis and Agricultural Biotechnology. 22:101382
The aim of this work was to determine the antimicrobial activity of chitooligosaccharides (chito) and comparing them with that of the standards broad spectrum antibiotic flomox and kluacid. The chito were prepared by enzyme hydrolysis of chitosan. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6236244f98405cc39c432b415312618e
https://doi.org/10.1016/j.bcab.2019.101382
https://doi.org/10.1016/j.bcab.2019.101382
Publikováno v:
Biocatalysis and Agricultural Biotechnology. 19:101123
The aim of the present study was to prepare novel monophenolase inhibitory peptides from Vicia faba (broad bean) pods. Isolated protein was hydrolysed by immobilized protease at pH 10. For maximum production of hydrolysate (peptides), an optimized hy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::50a4fe1cbe626f6f744e33ba36ba3112
https://doi.org/10.1016/j.bcab.2019.101123
https://doi.org/10.1016/j.bcab.2019.101123
Publikováno v:
International Journal of Food Science & Technology. 29:255-262
Properties of polygalacturonase [E.C. 3.2.1.15] (E 1 ) and invertase (E.C. 3.2.1.26] (E 2 ) isolated and purified in powdered form from Endomycopsis fibuligera grown on date wastes were measured. The molecular weights were estimated to be about 32 00
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c79887a86c9f545a039cd774a92cc31
https://doi.org/10.1111/j.1365-2621.1994.tb02067.x
https://doi.org/10.1111/j.1365-2621.1994.tb02067.x
Publikováno v:
Applied Biochemistry and Biotechnology. 55:219-230
Glycosidases namely myrosinase and β-amylase, have been isolated fromBrassicaceae. These enzymes were identified and estimated by the rate of glucose and maltose formation from sinigrin (thioglucosinolate) and amylose (polysaccharides) hydrolysis, r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1309d77f725bd194b2ee2430f7e2fb1e
https://doi.org/10.1007/bf02786861
https://doi.org/10.1007/bf02786861
Autor:
Sanaa T. El-Sayed, Etidal W. Jwanny
Publikováno v:
Applied Biochemistry and Biotechnology. 49:11-22
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::92394d2c2e5a33a81f29c6f941c89b40
https://doi.org/10.1007/bf02888843
https://doi.org/10.1007/bf02888843
Publikováno v:
Phytochemistry. 39:1301-1303
Two myrosinase isoenzymes ( EC 3. 2. 3. 1 ) were extracted and purified by (NH 4 ) 2 SO 4 precipitation and DEAE-cellulose and Sephadex G-200 chromatography from radish root tissues with M r s 28 800 and 58 900. The most active one (120 U mg −1 ) w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74f0a4bb12eddb47e5b4b04c3f370070
https://doi.org/10.1016/0031-9422(95)00099-s
https://doi.org/10.1016/0031-9422(95)00099-s
Akademický článek
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Autor:
K. I. Fayek, Sanaa T. El-Sayed
Publikováno v:
Zeitschrift für allgemeine Mikrobiologie. 20:383-387
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f8e9b6f7a1c71701ad632406a4eb07f
https://doi.org/10.1002/jobm.19800200604
https://doi.org/10.1002/jobm.19800200604