Enzymatic roles in nectar-to-honey transformation by the Indian honey bee, Apis cerana Fabricius.
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| Title: | Enzymatic roles in nectar-to-honey transformation by the Indian honey bee, Apis cerana Fabricius. |
|---|---|
| Authors: | V. S, Harithasree1 (AUTHOR), V, Vijayasree2 (AUTHOR) vijayasree.v@kau.in |
| Source: | Biocatalysis & Biotransformation. Jun2026, Vol. 44 Issue 3, p219-226. 8p. |
| Subjects: | Invertase, Glucose oxidase, Catalytic activity, Amylases, Honey composition, Catalase, Apis cerana |
| 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. [ABSTRACT FROM AUTHOR] |
| Copyright of Biocatalysis & Biotransformation is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 194165869 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Enzymatic roles in nectar-to-honey transformation by the Indian honey bee, Apis cerana Fabricius. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22V%2E+S%2C+Harithasree%22">V. S, Harithasree</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22V%2C+Vijayasree%22">V, Vijayasree</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> vijayasree.v@kau.in</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biocatalysis+%26+Biotransformation%22">Biocatalysis & Biotransformation</searchLink>. Jun2026, Vol. 44 Issue 3, p219-226. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Invertase%22">Invertase</searchLink><br /><searchLink fieldCode="DE" term="%22Glucose+oxidase%22">Glucose oxidase</searchLink><br /><searchLink fieldCode="DE" term="%22Catalytic+activity%22">Catalytic activity</searchLink><br /><searchLink fieldCode="DE" term="%22Amylases%22">Amylases</searchLink><br /><searchLink fieldCode="DE" term="%22Honey+composition%22">Honey composition</searchLink><br /><searchLink fieldCode="DE" term="%22Catalase%22">Catalase</searchLink><br /><searchLink fieldCode="DE" term="%22Apis+cerana%22">Apis cerana</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biocatalysis & Biotransformation is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1080/10242422.2026.2654542 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 219 Subjects: – SubjectFull: Invertase Type: general – SubjectFull: Glucose oxidase Type: general – SubjectFull: Catalytic activity Type: general – SubjectFull: Amylases Type: general – SubjectFull: Honey composition Type: general – SubjectFull: Catalase Type: general – SubjectFull: Apis cerana Type: general Titles: – TitleFull: Enzymatic roles in nectar-to-honey transformation by the Indian honey bee, Apis cerana Fabricius. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: V. S, Harithasree – PersonEntity: Name: NameFull: V, Vijayasree IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 06 Text: Jun2026 Type: published Y: 2026 Identifiers: – Type: issn-print Value: 10242422 Numbering: – Type: volume Value: 44 – Type: issue Value: 3 Titles: – TitleFull: Biocatalysis & Biotransformation Type: main |
| ResultId | 1 |
