Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.3 extracted from

  • Eldin, M.S.; Seuror, E.I.; Nasr, M.A.; Tieama, H.A.
    Affinity covalent immobilization of glucoamylase onto p-benzoquinone-activated alginate beads: II. Enzyme immobilization and characterization (2011), Appl. Biochem. Biotechnol., 164, 45-57.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information preparation of Ca-alginate gel beads, activation by p-benzoquinoone, and immobilization of purified enzyme, method, development, comparison of catalytic activities of free and immobilized enzyme, overview. Km values of free and entrapped glucoamylase are almost identical, while the covalently immobilized enzyme shows the lowest affinity for substrate. The covalently immobilized enzyme retains its activity over 36 days of shelf storage and after 30 repeated use runs Picrophilus torridus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Picrophilus torridus

Organism

Organism UniProt Comment Textmining
Picrophilus torridus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Picrophilus torridus
-

Synonyms

Synonyms Comment Organism
glucoamylase
-
Picrophilus torridus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
both free and immobilized enzymes Picrophilus torridus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2
-
both free and immobilized enzymes Picrophilus torridus

pH Range

pH Minimum pH Maximum Comment Organism
1 5 activity range of both free and immobilized enzymes, profiles, overview Picrophilus torridus