Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)
ΚΑΘΑΡΙΣΜΟΣ ΚΑΙ ΜΕΛΕΤΗ ΙΔΙΟΤΗΤΩΝ ΜΙΑΣ Β-ΓΛΥΚΟΣΙΔΑΣΗΣ ΚΑΙ ΜΙΑΣ Β-ΓΑΛΑΚΤΟΣΙΔΑΣΗΣ ΑΠΟ ΣΠΕΡΜΑΤΑ ΚΡΙΘΑΡΙΟΥ. ΕΦΑΡΜΟΓΗ ΤΩΝ ΕΝΖΥΜΩΝ ΣΤΗΝ ΥΔΡΟΛΥΣΗ ...
Abstract
dc:descriptionTWO ENZYMES A B-GLUCOSIDASE AND A B-GALACTOSIDASE WERE ISOLATED AND CHARACTERIZED FROM BARLEY SEEDS. THE B-GLUCOSIDASE IS A SINGLE BASIC POLYPEPTIDE (PI>8,5) WITH A MR OF 53.000 ACTING OPTIMALLY AT PH 4.5-5.0. THE B-GALACTOSIDASE IS COMPOSED OF TWO SUBUNITS WITH A MR OF 42.000 AND 33.000 RESPECTIVELY, IS ACIDIC IN NATURE (PI<5.7) AND ACTS OPTIMALLY AT PH 4.0. BOTH ENZYMES CAN HYDROLYZE LACTOSE, IN PURE SOLUTION OR IN WHEY, THEY ARE GLYCOPROTEINS THEY EXHIBIT CHARGE HETEROGENEITY AND CAN CATALYZE TRANSGALACTOSYLATION REACTIONS. B-GLUCOSIDASE WAS IMMOBILIZED ON SEPHAROSE, ON RESIN (DUOLITE) AND ON POROUS GLASS BEADS WITH SIGNIFICANT CONSERVATION OF ITS ACTIVITY. THE SEPHAROSE IMMOBILIZED ENZYME ACQUIRED INCREASED THERMOSTABILITY.
Degree
thesis:*- Grantor dc:publisher
- Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)
- Year dc:date
- 1990
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Σίμος, Γεώργιος
Subjects
dc:subject × 16- B-GALACTOSIDASE
- B-GLUCOSIDASE
- BARLEY (HORDEUM VULGARE)
- IMMOBILIZATION OF B-GLUCOSIDASE
- LACTOSE HYDROLYSIS
- TRANSGALACTOSYLATION
- Β-ΓΑΛΑΚΤΟΣΙΔΑΣΗ
- Β-ΓΛΥΚΟΣΙΔΑΣΗ
- ΚΑΘΗΛΩΣΗ (ΑΚΙΝΗΤΟΠΟΙΗΣΗ) Β-ΓΛΥΚΟΣΙΔΑΣΗΣ
- ΚΡΙΘΑΡΙ (HORDEUM VULGARE)
- ΤΡΑΝΣΓΑΛΑΚΤΟΣΥΛΙΩΣΗ
- ΥΔΡΟΛΥΣΗ ΛΑΚΤΟΖΗΣ
- Φυσικές Επιστήμες
- Natural Sciences
- Χημεία
- Chemical Sciences
Rights
- Language dc:language
- gre
Identifiers
dc:identifier.*- Identifier
- 10.12681/eadd/1305
- OAI identifier oai:identifier
- oai:10442/1305