Monascus pigments

Monascus pigments (MPs) as natural food colorants have been widely utilized in food industries in the world, especially in China and Japan. Moreover, MPs possess a range of biological activities, such as anti-mutagenic and anticancer properties, antimicrobial activities, potential anti-obesity activities, and so on. So, in the past two decades, more and more attention has been paid to MPs. Up to now, more than 50 MPs have been identified and studied. However, there have been some reviews about red fermented rice and the secondary metabolites produced by Monascus, but no monograph or review of MPs has been published. This review covers the categories and structures, biosynthetic pathway, production, properties, detection methods, functions, and molecular biology of MPs.     

Cone visual pigments

Cone visual pigments are visual opsins that are present in vertebrate cone photoreceptor cells and act as photoreceptor molecules responsible for photopic vision. Like the rod visual pigment rhodopsin, which is responsible for scotopic vision, cone visual pigments contain the chromophore 11-cis-retinal, which undergoes cis–trans isomerization resulting in the induction of conformational changes of the protein moiety to form a G protein-activating state. There are multiple types of cone visual pigments with different absorption maxima, which are the molecular basis of color discrimination in animals. Cone visual pigments form a phylogenetic sister group with non-visual opsin groups such as pinopsin, VA opsin, parapinopsin and parietopsin groups. Cone visual pigments diverged into four groups with different absorption maxima, and the rhodopsin group diverged from one of the four groups of cone visual pigments. The photochemical behavior of cone visual pigments is similar to that of pinopsin but considerably different from those of other non-visual opsins. G protein activation efficiency of cone visual pigments is also comparable to that of pinopsin but higher than that of the other non-visual opsins. Recent measurements with sufficient time-resolution demonstrated that G protein activation efficiency of cone visual pigments is lower than that of rhodopsin, which is one of the molecular bases for the lower amplification of cones compared to rods. In this review, the uniqueness of cone visual pigments is shown by comparison of their molecular properties with those of non-visual opsins and rhodopsin. This article is part of a Special Issue entitled: Retinal Proteins — You can teach an old dog new tricks.     

Photointermediates of visual pigments

Much progress has been made in recent years toward understanding the interactions between various proteins responsible for visual transduction which are initiated by an activated state of visual pigments. However, the changes which take place in the visual pigments themselves to convert them to the activated state are more poorly understood. Many spectroscopic techniques have been applied to this problem in recent years and considerable progress has been made. A major goal of these efforts is to understand at which stages protein change occurs and to characterize its structural features. In the visual system evidence is accumulating, for example, that chromophore independent protein change begins immediately prior to lumirhodopsin formation. Considerable insight has been gained recently into the early intermediates of visual transduction and the stage is set to achieve similar understanding of the later intermediates leading to rhodopsin's activated state.     

Lipid pigments and aging

It is a short survey of lipid pigment formation in which the role of free radicals in the peroxidation of lipids is particularly stressed. The chemical structure of lipopigments and the role of the chemical moiety in histochemical reactions is shortly overviewed. A new aspect of age in the formation of lipopigments is brought to light. Finally the role of hypoxaemia and no-reflow phenomenon influencing the pigment formation is discussed.     

Demetalation of chlorophyll pigments

Natural chlorophylls (Chls) and bacteriochlorophyll (BChls), which are major pigments in photosynthesis, possess a central Mg (or Zn) in their cyclic tetrapyrrole macrocycles. Removal of the central metal atom from chlorophyllous pigments, called pheophytinization, is a biologically important reaction in that it allows production of the primary electron acceptors in photosystem II(-type) reaction centers and is one of the crucial steps in the Chl degradation pathway. Pheophytinization in processed and postharvest foods derived from vegetables and fruits has attracted considerable attention in agricultural and food chemistry from the viewpoints of maintenance of their color level and evaluation by consumers. In this review, we focus on in vivo demetalation reactions and demetalated products of chlorophyllous pigments. In addition, we summarize kinetic studies on in vitro demetalation of natural (B)Chl molecules and their synthetic analogs under acidic conditions.     

Carotenoid pigments of Dioscorea cayenensis

The yellow flesh of Dioscorea cayenensis, a principal yam of Africa, was found to contain xanthophyll esters as the principal pigments. These included neoxanthin, violaxanthin and auroxanthin. In addition β-carotene, or pro-vitamin A was found in small quantities. Measurements show that D. cayenensis is a fair source of this nutrient.