Comparison of selective hydrolysis of α-lactalbumin by acid Protease A and Protease M as alternative to pepsin: potential for β-lactoglobulin purification in whey proteins
| Autor: | Ulrich Kulozik, Katarina Lisak Jakopović, Rajka Božanić, Seronei Chelulei Cheison |
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| Rok vydání: | 2019 |
| Předmět: |
Microbial enzymes
pepsin selective hydrolysis whey proteins 0106 biological sciences medicine.medical_treatment Lactoglobulins 01 natural sciences High-performance liquid chromatography Substrate Specificity Whey protein isolate Hydrolysis 0404 agricultural biotechnology Pepsin 010608 biotechnology medicine Lactalbumin chemistry.chemical_classification Protease biology Chemistry 04 agricultural and veterinary sciences General Medicine 040401 food science Pepsin A Kinetics Whey Proteins Enzyme Biochemistry biology.protein Kallikreins Animal Science and Zoology Digestion Peptide Hydrolases Food Science |
| Zdroj: | Journal of Dairy Research. 86:114-119 |
| ISSN: | 1469-7629 0022-0299 |
| DOI: | 10.1017/s0022029919000086 |
| Popis: | The experiments reported in this research paper examine the potential of digestion using acidic enzymes Protease A and Protease M to selectively hydrolyse α-lactalbumin (α-La) whilst leaving β-lactoglobulin (β-Lg) relatively intact. Both enzymes were compared with pepsin hydrolysis since its selectivity to different whey proteins is known. Analysis of the hydrolysis environment showed that the pH and temperature play a significant role in determining the best conditions for achievement of hydrolysis, irrespective of which enzyme was used. Whey protein isolate (WPI) was hydrolysed using pepsin, Acid Protease A and Protease M by randomized hydrolysis conditions. Reversed-phase high performance liquid chromatography was used to analyse residual proteins. Regarding enzyme selectivity under various milieu conditions, all three enzymes showed similarities in the reaction progress and their potential for β-Lg isolation. |
| Databáze: | OpenAIRE |
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