izpis_h1_title_alt

Stabilnost alfa-amilaze v različnih organizmih
ID Debevc, Janja (Author), ID Lah, Jurij (Mentor) More about this mentor... This link opens in a new window

.pdfPDF - Presentation file, Download (406,17 KB)
MD5: 10F72FC9599DF30E9D1F5EBCFDB3F156

Abstract
Primerjala sem stabilnostne krivulje, ki predstavljajo temperaturno odvisnost Gibbsove proste energije razvitja psihrofilnih, mezofilnih in termofilnih α-amilaz. Objavljeni rezultati kažejo, da je stabilnost največja pri termofilni α-amilazi in najmanjša pri psihrofilni α-amilazi. Razvidne so tudi različne temperature, pri katerih se razvijejo tako imenovane temperature taljenja. Najvišja je pri termofilni α-amilazi in najnižja pri psihrofilni α-amilazi.

Language:Slovenian
Keywords:α-amilaza, psihrofil, mezofil, termofil
Work type:Bachelor thesis/paper
Typology:2.11 - Undergraduate Thesis
Organization:FKKT - Faculty of Chemistry and Chemical Technology
Year:2019
PID:20.500.12556/RUL-111239 This link opens in a new window
COBISS.SI-ID:1538437571 This link opens in a new window
Publication date in RUL:26.09.2019
Views:1103
Downloads:210
Metadata:XML RDF-CHPDL DC-XML DC-RDF
:
Copy citation
Share:Bookmark and Share

Secondary language

Language:English
Title:Stability of alpha-amylase in different organisms
Abstract:
Stability curves representing the temperature dependence of the Gibbs free energy of the unfolding of psychophilic, mesophilic and thermophilic α-amylases are compared. The published results indicate that the stability is highest in the case of thermophilic α-amylase and lowest for psychophilic α-amylase. The unfolding transition temperatures, the so-called melting temperatures, are also evident. Melting temperature is highest for thermophilic α-amylase and lowest for psychophilic α-amylase.

Keywords:α-amylase, psihrophile, mesophile, thermophile

Similar documents

Similar works from RUL:
Similar works from other Slovenian collections:

Back