Floral nectar chitinase is a potential marker for monofloral honey botanical origin authentication: A case study from loquat (Eriobotrya japonica Lindl.).

Highlights • Bee-originated proteins are predominant proteinaceous components in loquat honey. • Loquat nectar proteome mainly consisted of xylosidase, thaumatin, and chitinase which were not detected in loquat honey. • The zymography of nectar-originated chitinases is a potential marker for honey botanical origin authentication. Abstract Honey, as a commercial product, is a target of adulteration through inappropriate production practices and deliberate mislabelling of botanical origin. Floral nectar protein could be a good marker for determining the source flowers of honey, especially monofloral honeys. Here, nectar and monofloral honey from Eriobotrya japonica Lindl. (loquat) were systematically compared, especially regarding proteomic and enzymatic activity. Using two-dimensional electrophoresis and mass spectrometry, only bee-originated proteins were detected in loquat honey. Xylosidase, thaumatin, and two kinds of chitinases were detected in loquat floral nectar, and their activity in loquat nectar and honey were quantified. Following gel electrophoresis, loquat honey had similar chitinase activity profiles to loquat nectar, but both were clearly distinguishable from Camellia sinensis nectar and Brassica napus honey. To our knowledge, this is the first examination of nectar-origin enzyme activity in honey. Zymography of chitinases is a potential marker for determining or authenticating the botanical origin of honeys. [ABSTRACT FROM AUTHOR]