Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor.
Goat whey was hydrolysed by pepsin in an ultrafiltration membrane enzymic reactor coupled with a 30 kDa mineral membrane. Peptides collected in the permeate were resolved using reversed-phase HPLC. Their sequences were determined by amino acid analysis, second order derivative spectra analysis and mass spectrometry. Owing to the resistance of beta-lactoglobulin (beta-lg) towards pepsin, the majority of peptides identified were derived from alpha-lactalbumin (alpha-la). Pepsin showed a broad specificity of hydrolysis sites and generated a wide range of products from dipeptides to very large peptides containing disulphide bridges. The molecular masses of peptides resulting from alpha-la degradation were between 150 and 6900 Da: 36% were < 600 Da. 24% were 600-2000 Da and 40% were > 2000 Da.
Bordenave
B S
BS
Laboratoire de Génie Protéique et Cellulaire, UPRES 2001, UFR Sciences, Université de La Rochelle, France. sbordena@univ-Lr.fr
Sannier
F
F
Ricart
G
G
Piot
J M
JM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006041:Goats; D006868:Hydrolysis; D007768:Lactalbumin / Q000737:chemistry* / Q000302:isolation & purification; D013058:Mass Spectrometry; D008567:Membranes, Artificial; D008894:Milk Proteins / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D010434:Pepsin A / Q000378:metabolism*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014462:Ultrafiltration; D000067816:Whey Proteins
D000596:Amino Acids; D008567:Membranes, Artificial; D008894:Milk Proteins; D000067816:Whey Proteins; D007768:Lactalbumin; D010434:Pepsin A