Vedecký časopis

Journal of Food and Nutrition Research
Online First Articles

Borutinskaite, V. – Treigyte, G. – Čeksteryte, V. – Kurtinaitiene, B. – Navakauskiene, R.
Proteomic identification and enzymatic activity of buckwheat (Fagopyrum esculentum) honey based on different assays

Violeta Čeksteryte, Institute of Agriculture, Lithuanian Research Centre for Agriculture and Forestry, Instituto aleja 1, LT-58344 Akademija, Lithuania. Tel: (+370) 672 18175, e-mail: violeta@lzi.lt

Received 31 May 2017; 1st revised 3 November 2017; 2nd revised 14 December 2017; accepted 19 December 2017

Súhrn: Buckwheat (Fagopyrum esculentum Moench) honey was analysed for enzymatic activity and proteomic content. Proteins were separated by one dimensional electrophoresis (1DE) in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) or resolved by two-dimensional gel electrophoresis (2DE). Using different mass spectrometry (MS) techniques, the main proteins of plant and honeybee Apis mellifera carnica, Pollmann origin were identified. Using direct MS analysis of honeybee proteome, a total of 87 proteins were identified in buckwheat honey. Proteins of honeybee origin included major royal jelly protein (MRJP), uncharacterized honeybee protein, high glutamic acid storage protein and enzymes alpha-glucosidase, alpha-amylase, glucosylceramidase. Separation of proteins by 1DE and 2DE revealed a smaller number of proteins, including 6 proteins of bee origin and 11 of yeast origin. In addition, catalase activity and glucose oxidase activity in buckwheat honey were estimated on the native PAGE. Our study provides a useful tool for the identification of honey proteins which play an important role in human nutrition and immune defence system.

Kľúčové slová: buckwheat honey; royal jelly; proteins; separation; two-dimensional electrophoresis; mass spectrometry