Corn gluten meal (CGM) was hydrolyzed by Alcalase after starch removal of CGM was applied as a pretreatment. A new inhibitory peptide for angiotensin I-converting enzyme (ACE) was isolated from the hydrolysate of CGM with the use of Bio-Rad P-2 gel filtration and followed by reverse-phase high-performance liquid chromatography (RP-HPLC). The sequence of the active peptide was determined to be Ala-Tyr after the application of amino acid analysis and HPLC/MS. The IC50 of the peptide was 14.2 microM, and it was not affected by preincubation with 30 mU of ACE at 37 degrees C for 3 h. Ala-Tyr also exerted antihypertensive effects after oral administration to spontaneously hypertensive rats. A maximal reduction of systolic blood pressure of 9.5 mmHg was observed 2 h after oral administration of Ala-Tyr at doses of 50 mg/kg.

A photodegradation study of Aflatoxin B(1) (AFB(1)) in water solution was performed under UV irradiation at different AFB(1) initial concentrations and UV irradiation intensities. The effect of UV intensity on the AFB(1) photodegradation ratio is dominative, when compared with AFB(1) initial concentration. The photodegradation of AFB(1) was proved to follow first-order reaction kinetics (R(2) > or = 0.99). Three photodegradation products, i.e. P(1) (C(17)H(14)O(7)), P(2) (C(16)H(14)O(6)) and P(3) (C(16)H(12)O(7)), were identified on the basis of low mass error and high matching property by ultra-performance liquid chromatography-quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF MS), and the degradation pathway was proposed. This study first reports the appearance of these photodegradation products and the proposed degradation pathway in aqueous media.

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