17β-Estradiol residues and estrogenic activities in the Hawkesbury River, Australia.

Two highly sensitive ELISAs for the specific detection of 17β-estradiol (E2) residues were developed, showing the limits of detection (LOD, a concentration at 15% inhibition of color development) of 0.04 ± 0.02 μg/L and 0.

A survey of 17α-ethinylestradiol and mestranol residues in Hawkesbury River, Australia, using a highly specific enzyme-linked immunosorbent assay (ELISA) demonstrates the levels of potential biological significance.

This study reports on the potential status of 17α-ethinylestradiol (EE2) and mestranol (MeEE2) residues in aquatic environments in New South Wales (NSW), Australia, based on the analysis by a specific ELISA we developed. Polyclonal antibodies were raised against the EE2 hapten with a linker attached at the C3-position to direct the antibody binding towards the ring D of EE2/MeEE2. Using this approach, an ELISA highly specific to EE2 and MeEE2 was successfully developed, showing less than 3.

In vitro digestion of rice bran proteins produces peptides with potent inhibitory effects on α-glucosidase and angiotensin I converting enzyme.

Background: The bioactivities of peptides released from the digestion of rice bran protein under in vitro simulated human digestive conditions were investigated. Four protein fractions extracted from rice bran were digested and the hydrolysates were fractionated by ultrafiltration and anion exchange chromatography. α-Glucosidase and angiotensin converting enzyme (ACE) inhibitory activities of the crude hydrolysates and their fractions were determined.

Rice bran protein hydrolysates exhibit strong in vitro α-amylase, β-glucosidase and ACE-inhibition activities.

Background: The objective of this study was to systematically examine the in vitro health-promotion activities of rice bran protein hydrolysates. Rice bran proteins were fractioned into albumin, globulin, prolamin and glutelin, which were subjected to hydrolysis by four protease preparations, namely Alcalase, Neutrase, Flavourzyme and Protamax, and the inhibitory activities of the hydrolysates against α-amylase, α-glucosidase and angiotensin converting enzyme (ACE), were monitored over a hydrolysis period of 240 min. Active peptides in the hydrolysates were isolated by ultra-filtration and ion-exchange chromatography and the peptide sequences of the active fractions were identified by LC-MS/MS.

A testosterone specific competitive enzyme immunoassay for monitoring water quality.

Testosterone, an androgen and a primary male sex hormone, migrates through the environment in ways which could pose a threat to water quality and, subsequently, environmental and human health. This paper describes the development of a direct competitive enzyme-linked immunosorbent assay (ELISA) that is capable of measuring testosterone with high specificity. The testosterone ELISA displayed the IC20 (as the limit of detection) and IC50 values of 0.