Journal
JOURNAL OF ANIMAL PHYSIOLOGY AND ANIMAL NUTRITION
Volume 98, Issue 5, Pages 830-837Publisher
WILEY-BLACKWELL
DOI: 10.1111/jpn.12140
Keywords
peanut meal protein hydrolysates; molecular weight distribution; endurance-enhancing capacity; endurance-enhancing peptide; identification
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To improve the functional properties of peanut meal protein for wide utilization, hydrolysis was conducted by alcalase. Compared with saline and peanut meal protein, intragastric administration of low molecular weight (<1kD) peanut meal peptide (PPH I) could significantly prolong swimming time, increase levels of blood sugar, non-esterified fatty acids (NEFA) and liver glycogen and decrease blood lactate content in mice. Levels of Pro, Leu, Val and His in low molecular weight peanut meal peptides were higher significantly than those in other peanut meal protein hydrolysates. Hydrophobic amino acids, such as Pro, Tyr and His, could perhaps capture free radical and increase antioxidant capacity of peanut peptide and retard fatigue induced by free radical. After separation by HPLC, a primary peptide P1, Pro-Glu-Ile-Glu-Val, was sequenced. Its N-terminal was Val, and it was rich in antioxidant amino acid, Pro and Ile. Levels of plasma glucose, NEFA and liver glycogen in PPH I group were higher than those in mice intragastric administration with peptide P1, and the swimming time is longer in PPH I group than in P1 group. So, the high content of P1 was one of the reason why PPH I had high endurance-enhancing capacity.
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