1. The origin of honey amylase
- Author
-
Carola Ponzetto, Maria Teresa Rinaudo, F. Marletto, and C. Vidano
- Subjects
Physiology ,Sambucus nigra ,medicine.disease_cause ,Hydroxylamines ,Biochemistry ,Animal origin ,Chloride ,Chlorides ,Drug Stability ,Pollen ,Botany ,medicine ,Nectar ,Animals ,Amylase ,Food science ,Molecular Biology ,chemistry.chemical_classification ,biology ,Robinia ,Temperature ,Acetylation ,General Medicine ,Honey ,Bees ,Hydrogen-Ion Concentration ,Plants ,biology.organism_classification ,Enzyme Activation ,Enzyme ,chemistry ,Amylases ,biology.protein ,medicine.drug - Abstract
1. 1. Robinia pseudo-acacia honey and Apis mellifera food gland amylase display optimal activity at pH 5·6–5·9 and 45°C, with a persistent feeble activity at 80°C. The chloride ions (0·1 M) are the activators of both enzymes. 2. 2. R. pseudo-acacia nectar and Sambucus nigra pollen amylase, on the other hand, displayed well-marked pH peaks at 7·2 and 5·9 respectively. The optimum temperature was 45°C, with total inactivity at 75°C. 3. 3. It is therefore considered that honey amylase may be treated as being of animal origin.
- Published
- 1973