Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor

被引：9

作者：

Bordenave, S

Sannier, F

Ricart, G

Piot, JM

机构：

[1] Univ La Rochelle, UFR Sci, UPRES 2001, Lab Genie Prot & Cellulaire, F-17042 La Rochelle 01, France

[2] Univ Sci & Tech Lille Flandres Artois, Lab Spectrometrie Masse, F-59655 Villeneuve Dascq, France

来源：

JOURNAL OF DAIRY RESEARCH | 2000年 / 67卷 / 04期

关键词：

D O I：

10.1017/S0022029900004416

中图分类号：

S8 [畜牧、动物医学、狩猎、蚕、蜂];

学科分类号：

0905 ;

摘要：

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 mas 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.

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页码：551 / 559

页数：9

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