undergraduate thesis
Barley Albumins and Globulins Electrophoretic Protein Pattern as Affected by Different Extraction Solvents

Anita Kolaković (2013)
Josip Juraj Strossmayer University of Osijek
FACULTY OF FOOD TECHNOLOGY
Department of Applied Chemistry and Ecology
Sub-department of Biochemistry and Toxicology
Metadata
TitleUtjecaj različitih otapala na elektroforetski profil albumina i globulina ječma
AuthorAnita Kolaković
Mentor(s)Ivica Strelec (thesis advisor)
Abstract
Cilj ovog rada je bio ustanoviti kako različita otapala utječu na ekstraktibilnost albumina i globulina ječma te ustanoviti njihov utjecaj na raspored proteinskih vrpci po provedenoj SDS - PAGE. Albumini ječma su ekstrahirani MilliQ vodom, globulini ječma 0,5 M NaCl slijednom ekstrakcijom nakon ekstrakcije albumina, a albuminsko-globulinska frakcija proteina pomoću dva različita otapala: 50 mM Tris-HCl pufera pH 8,0 i 0,5 M NaCl. Rezultati su pokazali da se stupnjevitom ekstrakcijom albumina i globulina iz ječma ekstrahira podjednaka količina albumina i globulina, pri čemu albumini čine 53 ± 1 %, a globulini 47 ± 1% od sume ovih dviju frakcija proteina. Primjenom direktne ekstrakcije albuminsko/globulinske frakcije pomoću 50 mM Tris-HCl pufera pH 8,0, ili 0,5 M NaCl ekstrahirana je količina proteina jednaka sumi stupnjevito ekstrahiranih albumina i globulina. Primijenjeno ekstrakcijsko otapalo pokazalo je značajan učinak na raspored proteinskih vrpci albumina, globulina i albuminsko/globulinske frakcije proteina ječma po provedenoj SDS-PAGE. Albumineje od globulina bilo moguće razlikovali po proteinskim vrpcama u rasponu molekulskih masa između 20 i 45 kDa, te nedostatkom proteinske vrpce molekulske mase 59 kDa.Albuminsko/globulinska frakcija proteina sadržavala je sve proteinske vrpce uočene u albuminskoj i globulinskoj frakciji proteina. Albuminsko/globulinske frakcije proteina ječma ekstrahirane pomoću 50 mM Tris-HCl pufera pH 8,0, ili 0,5 M NaCl pokazivale su gotovo identičan raspored proteinskih vrpci, s tim da je albuminsko/globulinska frakcija ekstrahirana pomoću 50 mM Tris-HCl pufera pH 8,0 pokazivala dodatnu proteinsku vrpcu molekulske mase 140 kDa, a albuminsko/globulinska frakcija ekstrahirana pomoću 0,5 M NaCl znatno intenzivniju proteinsku vrpcu molekulske mase 59 kDa.
Keywordsbarley proteins
Parallel title (English)Barley Albumins and Globulins Electrophoretic Protein Pattern as Affected by Different Extraction Solvents
GranterJosip Juraj Strossmayer University of Osijek
FACULTY OF FOOD TECHNOLOGY
Lower level organizational unitsDepartment of Applied Chemistry and Ecology
Sub-department of Biochemistry and Toxicology
PlaceOsijek
StateCroatia
Scientific field, discipline, subdisciplineBIOTECHNICAL SCIENCES
Food Technology
Engineering
Study programme typeuniversity
Study levelundergraduate
Study programmeFood Technology
Academic title abbreviationuniv. bacc. ing. techn. aliment.
Genreundergraduate thesis
Language Croatian
Defense date2013-09-30
Parallel abstract (English)
Influence of different extraction solvents on barley flour albumins and globulins concentration, as well as albumin and globulin electrophoretic protein pattern obtained after SDS-PAGE was investigated. Albumins were extracted with Milli Q water, globulins with 0.5 M NaCl sequentially after albumin extraction, while albumin/globulin protein fraction directly by 50 mM Tris-HCl buffer pH 8.0 or 0.5 M NaCl. Results showed that almost the same amount of albumins and globulins were extracted from barley flour by sequential extraction. Extracted albumins presented 53 ± 1 % and globulins 47 ± 1% of the sum of these two protein fractions. Protein concentration equal to the sum of sequentially extracted albumins and globulins was obtained when direct extraction of albumin/globulin protein fractions by 50 mM Tris-HCl buffer pH 8.0 or 0.5 M NaCl were performed. Extraction solvent significantly influenced SDS-PAGE electrophoretic protein pattern of albumins, globulins and albumin/globulin protein fraction. Albumins could be discriminated from globulins by several proteins bands in the range of 20 to 45 kDa, as well as by the absence of protein band around 59 kDa which was present in globulin pattern. Electrophoretic pattern of albumin/globulin protein fractions contained all protein bands observed in albumin and globulin protein fractions alone. Although albumin/globulin protein fractions extracted by 50 mM Tris-HCl buffer pH 8.0 or 0.5 M NaCl showed almost identical protein pattern, slight differences between these two fractions could be observed. Albumin/globulin protein fraction extracted by 50 mM Tris-HCl buffer pH 8.0 had additional protein band around 140 kDa, while those one extracted by 0.5 M NaCl showed more intense protein band around 59 kDa.
Parallel keywords (Croatian)proteini ječma
Resource typetext
Access conditionAccess restricted to students and staff of home institution
Terms of usehttp://rightsstatements.org/vocab/InC/1.0/
URN:NBNhttps://urn.nsk.hr/urn:nbn:hr:109:441660
CommitterIvana Šuvak