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undergraduate thesis
Svojstva, modifikacije i primjena saharoza fosforilaze
Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology, 2020. urn:nbn:hr:159:076394
Vrtodušić, Lucija
University of Zagreb
Faculty of Food Technology and Biotechnology
Department of Biochemical Engineering
Laboratory for Biochemical Engineering, Industrial Microbiology and Malting and Brewing Technology

Institutional repository: Repository of the Faculty of Food Technology and Biotechnology

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Vrtodušić, L. (2020). Svojstva, modifikacije i primjena saharoza fosforilaze (Undergraduate thesis). Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:159:076394

Vrtodušić, Lucija. "Svojstva, modifikacije i primjena saharoza fosforilaze." Undergraduate thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2020. https://urn.nsk.hr/urn:nbn:hr:159:076394

Vrtodušić, Lucija. "Svojstva, modifikacije i primjena saharoza fosforilaze." Undergraduate thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2020. https://urn.nsk.hr/urn:nbn:hr:159:076394

Vrtodušić, L. (2020). 'Svojstva, modifikacije i primjena saharoza fosforilaze', Undergraduate thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, accessed 29 June 2024, https://urn.nsk.hr/urn:nbn:hr:159:076394

Vrtodušić L. Svojstva, modifikacije i primjena saharoza fosforilaze [Undergraduate thesis]. Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology; 2020 [cited 2024 June 29] Available at: https://urn.nsk.hr/urn:nbn:hr:159:076394

L. Vrtodušić, "Svojstva, modifikacije i primjena saharoza fosforilaze", Undergraduate thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, Zagreb, 2020. Available at: https://urn.nsk.hr/urn:nbn:hr:159:076394

Metadata
TitleSvojstva, modifikacije i primjena saharoza fosforilaze
Title (english)Properties, modifications and employment of sucrose phosphorylase
AuthorLucija Vrtodušić
MentorAnita Slavica (mentor)
GranterUniversity of Zagreb
Faculty of Food Technology and Biotechnology
(Department of Biochemical Engineering)
(Laboratory for Biochemical Engineering, Industrial Microbiology and Malting and Brewing Technology)
Zagreb
Defense date and country2020-07-01, Croatia
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Abstract
Saharoza fosforilaza (EC 2.4.1.7) je bakterijska citosolna glikoziltransferaza. U reakciji sa supstratom ovaj enzim formira kompleks β-glukozil-enzim, koji može sudjelovati u četiri različite reakcije: fosforolizi, sintezi, hidrolizi i transglukozilaciji. U reakciji fosforolize u reakciji s ortofosfatom nastaje α-D-glukoza-1-fosfat, a u suprotnom smjeru se odvija reakcija sinteze supstrata - donora glukozila. Do hidrolize kompleksa β-glukozil-enzim dolazi u reakciji s vodom i nastaje glukoza. Transglukozilacijom se glukozil od donora prenosi na različite molekule akceptora, pri čemu nastaju visoko vrijedni α-konfigurirani glukozilirani spojevi. Saharoza fosforilaza katalizira opisane reakcije ping-pong mehanizmom tipa Bi-Bi. Primjenom točkastih mutacija okarakterizirana su tri ključna bočna lanca aminokiselina u aktivnom mjestu saharoza fosforilaze: Asp-192 (katalitički nukleofil), Glu-232 (katalitička kiselina/baza) i Asp-290 (stabilizator prijelaznog stanja). Preostaje da se naprave mutanti ovog enzima koji imaju zadovoljavajuću stabilnost u uvjetima industrijske proizvodnje i na taj način proizvode visokovrijedni glukozilirani proizvodi s širokom primjenom u prehrambenoj, farmaceutskoj i kozmetičkoj industriji.
Abstract (english)
Sucrose phosphorylase (EC 2.4.1.7) is a bacterial cytosolic glycosyltransferase. β-glucosyl-enzyme complex formed in a reaction of this enzyme with a substrate can be used in four different reactions: phosphorolysis, synthesis, hydrolysis and transglucosylation. α-D-glucose-1-phosphate is produced in a reaction of the complex and an orthophosphate (phosphorolysis). Substrate (glucosyl donor) can be synthesized in opposite direction of phosphorolysis. During transglucosylation glucosyl moiety is transferred from a donor to an acceptor molecule and different high-added value glucosylated compounds can be yielded in this reaction. Ping-pong Bi-Bi mechanism is characteristic for reactions catalysed by the sucrose phosphorylase. Site directed mutagenesis was used to determine three key amino acid side chains in active site of the enzyme: Asp-192 (catalytic nucleophile), Glu-232 (catalytic acid/base) and Asp-290 (stabilizer of the complex). It remains to be seen if mutants with satisfactory stability under industrial conditions will be produced and used in manufacturing of high-added value glycosylated products with versatile applications in industry.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:159:076394
Study programmeTitle: Biotechnology
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) inženjer/inženjerka biotehnologije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) inženjer/inženjerka biotehnologije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence Attribution-NoDerivatives 4.0 International (CC BY-ND 4.0) icon
Created on2020-07-09 10:33:26