Search

This research intends to reveal the effects of different storage temperatures on the HMF amounts and diastase activities of strained flower honey and honeydew honey samples produced by different companies in Turkey. In this context, the initial HMF values and diastase activities of the strained flower honey and honeydew honey samples belonging to five different companies, collected at the date of filling, were examined with defined quality criteria (moisture, sugar, pH, acidity, electrical conductivity and ash). Samples were stored at certain temperatures (10±2 °C, 22±2 °C, 35±2 °C), and were analyzed at the end of each of the threemonth periods (3rd, 6th, 9th and 12th months) regarding HMF and diastase activity. According to the results, average HMF values of the flower honey and honeydew honey samples stored at 10±2 °C and 22±2 °C for one year did not exceed 40 mg/kg, which is given as the limit HMF value in the Turkish Food Codex (TFC) Directive on honey, while it rapidly increased in the samples stored at 35±2 °C, and was determined to be over 40 mg/kg as of 6th month onwards. In addition, average diastase activities of the samples at 10±2 °C and 22±2 °C did not drop below the limit value of 8 in TFC, though it was determined to be below 8 as of 6th month onwards, for the flower honey stored at 35±2 °C. To conclude, decrease in diastase activity shortens the shelf lives set by the firms. By providing proper production and storage conditions, all quality criteria should be ensured to remain consistent with the TFC Directive on honey. [ABSTRACT FROM AUTHOR]

α-Amylase was extracted from honeydew honey and purified by CM-Toyopearl 650M and Toyopearl HW-55F column chromatographies. The molecular weight of the enzyme was estimated to be about 58 kDa by Toyopearl HW-55F gel chromatography and SDS-PAGE, respectively. The optimum pH was 4.0 and optimum temperature 50°C. Inactivation of the enzyme occured when the pH was higher than 8.0 or lower than 3.0. This enzyme activated by Ca2+ and Mn2+, but inhibited by Fe3+, Hg2+, Zn2+, and EDTA. TLC analysis also suggested that the purified enzyme was of the α-type. The relative rate of hydrolysis of the polymeric substance decreased with decreasing percentage of α-1,4-linkages and with increasing percentage of α-1,6-linkages in substrate. [ABSTRACT FROM AUTHOR]

Honey adulteration is a common practice that deceives consumers and devalues the unique curative and food properties of honey. For marketing, each honey must satisfy an internationally valid Codex standard. One of the quality parameters is diastase/amylase activity, which, if lowered, may be compensated for by the addition of foreign amylases. However, the estimation of enzyme activity does not enable identification of artificially added amylases. 45 honey samples were analyzed using label-free nanoLC-MS/MS proteomics. Four honeys were found to contain the foreign amylases from Aspergillus niger, Bacillus amyloliquefaciens and/or Bacillus licheniformis. This result was confirmed via proof of specificity at multiple levels. Furthermore, we identified a series of plant-related protein groups. Despite plant-related proteins constituting a significant portion of honey proteins, they were minor components compared to the major honey bee-derived proteins. Bioinformatic analysis also provided evidence for aphid and catalase proteins in honey, but the limited specificity of the MS/MS identified peptides must be considered. Overall, we demonstrate a proteomics approach employing LC-MS/MS that is useful for proving adulteration and assessing honey quality. As an resource useful for reference, we provide curated sequence databases. In addition, we provide many markers that are naturally found in honey for future studies. Honey is unique natural product used since ancient times as a food and natural medicine. Humans strive to understand honey components because they can characterize different types of honey and be used for authentication and origin assessment. One of the important honey components are proteins. The proteins present in honey can naturally occur in honey, but some of them can be used to mask deficiencies in some honey quality properties. Diastases/amylases are such proteins, and their activity, a measure of honey freshness, can decrease in time or due to processing. To our knowledge, we for the first time specifically identify foreign amylases in honey. However, this study provided new information on other non-honey bee proteins in honey. Thus, this study is also of importance due to its identification of plant and aphid proteins and catalase-related proteins. This study provides a clue explaining the controversial presence of catalase in honey, since catalases can be identified and their origin determined via proteomics. [Display omitted] • Label-free proteomics enables comprehensive identification of markers in honey. • Proteomics accurately identifies artificially added amylases to adulterated honey. • We found that three different amylases were used to adulterate investigated honeys. • The approach we present can meet the need for accurate honey authentication. • An array of plant-, aphid- and catalase-related protein hits were found. [ABSTRACT FROM AUTHOR]