Proteomic and Glucosinolate Profiling of Rapeseed Isolates from Meals Produced by Different Oil Extraction Processes

Vassilios Raikos, Madalina Neacsu, Garry Duthie, Fergus Nicol, Martin Reid, Louise L. Cantlay, Viren Ranawana

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Abstract

The proteomes and glucosinolate content of two commercial rapeseed meals produced by cold-pressing and pre-press solvent extraction were investigated with the aim of identifying process-related differences between them. One-dimensional protein electrophoresis of the meals and their corresponding protein isolates revealed similarities in protein band distribution between cold-pressed and pre-press solvent extracted samples. Two-dimensional protein electrophoresis coupled with mass spectrometry confirmed that the seed storage protein cruciferin was the major protein in both meals either intact or in the form of α- and β- polypeptide subunits. HPLC analysis indicated that cold-press meals contained significantly higher amounts of glucosinolates than the solvent-extracted meals. Progoitrin was the main glucosinolate detected irrespective of the processing method used for extraction and levelled to 2.52 g/kg and 1.25 g/kg for cold-pressed and solvent–extracted meal respectively. Furthermore, glucosinolate-free protein isolates were prepared from this by-product of the oil production industry.
Original languageEnglish
Article numbere13060
JournalJournal of Food Processing and Preservation
Volume41
Issue number4
Early online date14 Sep 2016
DOIs
Publication statusPublished - Aug 2017

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Glucosinolates
Brassica rapa
glucosinolates
rapeseed
Proteomics
proteomics
Meals
Oils
Proteins
oils
protein isolates
electrophoresis
proteins
progoitrin
Electrophoresis
rapeseed meal
seed storage proteins
pressing
proteome
processing technology

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title = "Proteomic and Glucosinolate Profiling of Rapeseed Isolates from Meals Produced by Different Oil Extraction Processes",
abstract = "The proteomes and glucosinolate content of two commercial rapeseed meals produced by cold-pressing and pre-press solvent extraction were investigated with the aim of identifying process-related differences between them. One-dimensional protein electrophoresis of the meals and their corresponding protein isolates revealed similarities in protein band distribution between cold-pressed and pre-press solvent extracted samples. Two-dimensional protein electrophoresis coupled with mass spectrometry confirmed that the seed storage protein cruciferin was the major protein in both meals either intact or in the form of α- and β- polypeptide subunits. HPLC analysis indicated that cold-press meals contained significantly higher amounts of glucosinolates than the solvent-extracted meals. Progoitrin was the main glucosinolate detected irrespective of the processing method used for extraction and levelled to 2.52 g/kg and 1.25 g/kg for cold-pressed and solvent–extracted meal respectively. Furthermore, glucosinolate-free protein isolates were prepared from this by-product of the oil production industry.",
author = "Vassilios Raikos and Madalina Neacsu and Garry Duthie and Fergus Nicol and Martin Reid and Cantlay, {Louise L.} and Viren Ranawana",
note = "Acknowledgment This work is part of the Strategic Research 2011–2016 and is funded by the Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS).",
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T1 - Proteomic and Glucosinolate Profiling of Rapeseed Isolates from Meals Produced by Different Oil Extraction Processes

AU - Raikos, Vassilios

AU - Neacsu, Madalina

AU - Duthie, Garry

AU - Nicol, Fergus

AU - Reid, Martin

AU - Cantlay, Louise L.

AU - Ranawana, Viren

N1 - Acknowledgment This work is part of the Strategic Research 2011–2016 and is funded by the Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS).

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Y1 - 2017/8

N2 - The proteomes and glucosinolate content of two commercial rapeseed meals produced by cold-pressing and pre-press solvent extraction were investigated with the aim of identifying process-related differences between them. One-dimensional protein electrophoresis of the meals and their corresponding protein isolates revealed similarities in protein band distribution between cold-pressed and pre-press solvent extracted samples. Two-dimensional protein electrophoresis coupled with mass spectrometry confirmed that the seed storage protein cruciferin was the major protein in both meals either intact or in the form of α- and β- polypeptide subunits. HPLC analysis indicated that cold-press meals contained significantly higher amounts of glucosinolates than the solvent-extracted meals. Progoitrin was the main glucosinolate detected irrespective of the processing method used for extraction and levelled to 2.52 g/kg and 1.25 g/kg for cold-pressed and solvent–extracted meal respectively. Furthermore, glucosinolate-free protein isolates were prepared from this by-product of the oil production industry.

AB - The proteomes and glucosinolate content of two commercial rapeseed meals produced by cold-pressing and pre-press solvent extraction were investigated with the aim of identifying process-related differences between them. One-dimensional protein electrophoresis of the meals and their corresponding protein isolates revealed similarities in protein band distribution between cold-pressed and pre-press solvent extracted samples. Two-dimensional protein electrophoresis coupled with mass spectrometry confirmed that the seed storage protein cruciferin was the major protein in both meals either intact or in the form of α- and β- polypeptide subunits. HPLC analysis indicated that cold-press meals contained significantly higher amounts of glucosinolates than the solvent-extracted meals. Progoitrin was the main glucosinolate detected irrespective of the processing method used for extraction and levelled to 2.52 g/kg and 1.25 g/kg for cold-pressed and solvent–extracted meal respectively. Furthermore, glucosinolate-free protein isolates were prepared from this by-product of the oil production industry.

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