Looking for peptides from rice starch processing by-product: Bioreactor production, anti-tyrosinase and anti-inflammatory activity, and in silico putative taste assessment.

One of the major challenges for the modern society, is the development of a sustainable economy also aiming at the valorization of agro-industrial by-products in conjunction with at a significant reduction of generated residues from farm to retail. In this context, the present study demonstrates a biotechnological approach to yield bioactive peptides from a protein fraction obtained as a by-product of the rice starch production. Enzymatic hydrolysis, with the commercial proteases Alcalase and Protamex, were optimized in bioreactor up to 2 L of volume. The two best digestates, selected with respect to peptide release and extract antioxidant capacity, were further fractionated (cut-offs of 10, 5, and 1 kDa) via cross-flow filtration. Amino acid composition indicated that most of the fractions showed positive nutritional characteristics, but a putative bitter taste. A fraction obtained with Alcalase enzyme (retentate 8 kDa) exerted anti-inflammatory potential, while the smaller molecular weight fractions (retentate 1-5 kDa and permeate < 1 kDa) were more active in tyrosinase inhibition. The latter were further sub-fractionated by size-exclusion chromatography. From the 15 most anti-tyrosinase sub-fractions, 365 peptide sequences were identified via liquid chromatography coupled with high resolution mass spectrometry. The present data support the possible exploitation of bioactive peptide from rice starch by-product as ingredients into food, nutraceutical, pharmaceutical, and cosmetic formulations.

Peptide Fractions Obtained from Rice By-Products by Means of an Environment-Friendly Process Show In Vitro Health-Related Bioactivities.

Recently, the isolation of new health-related bioactive molecules derived from agro-food industrial by-products by means of environment-friendly extraction processes has become of particular interest. In the present study, a protein by-product from the rice starch industry was hydrolysed with five commercial proteolytic enzymes, avoiding the use of solvents or chemicals. The digestion processes were optimised, and the digestates were separated in fractions with four different molecular weight ranges by using a cross-flow membrane filtration technique. Total hydrolysates and fractions were tested in vitro for a wide range of biological activities. For the first time rice-derived peptides were assayed for anti-tyrosinase, anti-inflammatory, cytotoxicity and irritation capacities. Antioxidant and anti-hypertensive activities were also evaluated. Protamex, Alcalase and Neutrase treatments produced peptide fractions with valuable bioactivities without resulting cytotoxic or irritant. Highest levels of bioactivity were detected in Protamex-derived samples, followed by samples treated with Alcalase. Based on the present results, a future direct exploitation of isolated peptide fractions in the nutraceutical, functional food and cosmetic industrial fields may be foreseen.

Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution.

The plant light-harvesting complex of photosystem II (LHC-II) collects and transmits solar energy for photosynthesis in chloroplast membranes and has essential roles in regulation of photosynthesis and in photoprotection. The 2.5 A structure of pea LHC-II determined by X-ray crystallography of stacked two-dimensional crystals shows how membranes interact to form chloroplast grana, and reveals the mutual arrangement of 42 chlorophylls a and b, 12 carotenoids and six lipids in the LHC-II trimer. Spectral assignment of individual chlorophylls indicates the flow of energy in the complex and the mechanism of photoprotection in two close chlorophyll a-lutein pairs. We propose a simple mechanism for the xanthophyll-related, slow component of nonphotochemical quenching in LHC-II, by which excess energy is transferred to a zeaxanthin replacing violaxanthin in its binding site, and dissipated as heat. Our structure shows the complex in a quenched state, which may be relevant for the rapid, pH-induced component of nonphotochemical quenching.