Enzymatic roles in nectar-to-honey transformation by the Indian honey bee, Apis cerana Fabricius
Abstract
Enzymatic components from both bee secretions and floral sources are crucial for nectar-to-honey transformation, significantly influencing each stage of honey maturation and contributing to the complex biochemical reactions that underpin honey’s unique therapeutic properties. This study investigated variations in diastase, invertase, glucose oxidase, and catalase activities during honey formation in the Indian Honey Bee (Apis cerana Fabricius) fed on nectar from Pumpkin (Cucurbita moschata Poir.) and Rubber (Hevea brasiliensis Muell-Arg.). It was found that diastase and invertase, primarily derived from bee secretions, reached peak activity in the honey stomach (43.82 DN and 56.72 IN), where complex sugars are converted into simpler, energy-rich forms. Another bee-derived enzyme, glucose oxidase, showed high activity in early stages, while plant-derived catalase varied with nectar source and composition; together, these enzymes contribute to honey’s antimicrobial properties. Correlation analysis revealed positive links between diastase and invertase (r = 0.98), and glucose oxidase and catalase (r = 0.42) in both pumpkin and rubber honey, highlighting a synergistic biochemical interaction that defines honey’s exceptional characteristics. Findings indicate that diastase, invertase, and glucose oxidase are endogenous products of the bee’s hypopharyngeal and post-cerebral glands, in contrast to catalase, which is an exogenous enzyme of floral origin. These insights into enzyme origin and phase-specific activity deepen our understanding of honey’s biochemical transformation, providing a foundation for enhanced quality control and applications.
Fields of Study & Subjects
Insect and Arachnid Ecology and Behavior
Insect and Pesticide Research
Bee Products Chemical Analysis
Publication details
- Journal / source
- Biocatalysis and Biotransformation
- Publisher
- Informa UK Limited
- Volume
- 44
- Issue
- 3
- Pages
- 219–226
- Publication date
- 11 April 2026
- Language
- EN