Extraction and functionality of membrane-concentrated protein from defatted Rosa rubiginosa seeds

摘要

Rosa rubiginosa protein was extracted either with distilled water or in the presence of 0.5 M NaCl and further concentrated by ultrafiltration membranes. Temperature and pH influenced the extractability both protein and polyphenolic compounds. Up to 55-60/100 of the initial protein was solubilized during alkaline extraction. More than 90/100 of the solubilized protein was recovered in the unwashed concentrate, which contained more than 80/100 pure protein (d.b.).