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Isolation and Characterization of Invertase from Iraqi Date Fruit
Author(s) -
MAROUF BAHA A.,
ZEKI LIHAD
Publication year - 1982
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1982.tb10153.x
Subject(s) - invertase , sucrose , chemistry , enzyme , biochemistry , sodium , sodium dodecyl sulfate , chromatography , food science , organic chemistry
Soluble invertase was isolated and characterized from the pericarp of Iraqi date fruit, Sayer variety. The optimum pH of the soluble invertase was 4.0–4.7 and the optimum temperature was 50°C. The specific activity of the partially purified soluble invertase was 70.0 units per mg protein. The molecular weight of the soluble invertase was 70.0 units per mg protein. The molecular weight of the soluble invertase was probably more than 300,000 Daltons, and had high affinity for sucrose with a Km value of 3.33 × 10 ‐3 mM. Sodium dodecyl sulfate (SDS) inhibited the activity of the soluble invertase.