Use of macroporous adsorption resin for simultaneous desalting and debittering of whey protein hydrolysates

被引:48
作者
Cheison, Seronei C.
Zhang, Wang
Xu, Shi-Ying
机构
[1] So Yangtze Univ, Sch Food Sci, Key Lab Food Sci & Safety, Minist Educ, Wuxi 214036, Peoples R China
[2] Maseno Univ, Sch Publ Hlth & Community Dev, Maseno 40105, Kenya
关键词
angiotensin-I converting enzyme inhibition; bioactive peptides; debitter; desalt; hydrophobicity; macroporous adsorption resin; whey protein hydrolysate;
D O I
10.1111/j.1365-2621.2006.01461.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Whey protein isolate (WPI) was hydrolysed to whey protein hydrolysates (WPH) of degree of hydrolysis equal to 15% using Protease N 'Amano' G (IUB 3.4.24.28) in a batch reactor at 55 degrees C and pH 7.0 according to the pH-stat procedure. Ash was removed by adsorbing WPH onto macroporous adsorption resins (MAR). Following rinsing with deionised water, desorption was achieved by washing with 20%, 40% and 75% alcohol (v v(-1)) to obtain the three fractions HS20, HS40 and HS75. Ash reduced from 15.71% (WPH) to 4.38% (HS20), 2.02% (HS40) and 2.38% (HS75). Similarly, the protein content was enriched from a low of 64.89% (WPH) to 94.74% (HS20), 95.32% (HS40) and 92.00% (HS75). The fractions were analysed for surface hydrophobicity (SHo), angiotensin-I converting enzyme (ACE) inhibition, emulsifying activity index, total amino acids composition and molecular weight distribution. Fraction HS75 was objectionably bitter, showed superior ACE inhibition (lowest IC50), had the highest content of hydrophobic and essential amino acids and contained about 71% of < 600 Da with no fractions exceeding 4142 Da. Desorption with alcohol weakened the hydrophobic interaction forces between the peptides and resins and hence eluted the peptides, with the bitter HS75 being extracted.
引用
收藏
页码:1228 / 1239
页数:12
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