Cereal Chem. 94(1):58-65Pulses (Fabaceae) have regained interest for their high protein level. However, food application of pulses and pulse ingredients is hampered by several issues around their off-flavor. Off-flavors in pulses are partially inherent and partially produced during harvesting, processing, and storage. Generally, volatile off-flavor compounds in pulses belong to the categories of aldehydes, alcohols, ketones, acids, pyrazines, sulfur compounds, and others, and off-taste is strongly correlated to the presence of saponins, phenolic compounds, and sometimes alkaloids. No systematic studies have been performed on the identification of the off-flavor compounds present in pulses in relation to their contribution to the overall perception of the pulses. This review article aims to provide a concise overview highlighting the most important aspects of the knowledge available on the off-flavor compounds present in various pulses, their possible origins, and the technologies available to prevent, reduce, or mask these off-flavor compounds. Rather than attempting to make a full inventory of the literature in the field, this paper addresses the most relevant topics referring to a selected set of relevant papers on each topic to substantiate the observations and conclusions that may guide the reader toward additional literature.

Protease inhibitors from potato juice of cv. Elkana were purified and quantified. The protease inhibitors represent ca. 50% of the total soluble proteins in potato juice. The protease inhibitors were classified into seven different families: potato inhibitor I (PI-1), potato inhibitor II (PI-2), potato cysteine protease inhibitor (PCPI), potato aspartate protease inhibitor (PAPI), potato Kunitz-type protease inhibitor (PKPI), potato carboxypeptidase inhibitor (PCI), and "other serine protease inhibitors". The most abundant families were the PI-2 and PCPI families, representing 22 and 12% of all proteins in potato juice, respectively. Potato protease inhibitors show a broad spectrum of enzyme inhibition. All the families (except PCI) inhibited trypsin and/or chymotrypsin. PI-2 isoforms exhibit 82 and 50% of the total trypsin and chymotrypsin inhibiting activity, respectively. A strong variation within the latter activities was shown within one family and between protease inhibitor families.

The one-letter code system proposed here is a simple method to accurately describe structurally diverse oligosaccharides derived from heteroxylans. Substitutions or ‘molecular decoration(s)’ of main-chain d-xylosyl moieties are designated by unique letters. Hence, an oligosaccharide is described by a series of single letters, beginning with the non-reducing d-xylosyl unit. Superscripted numbers are used to indicate the linkage position(s) of main-chain substitution(s) and, where necessary, superscripted lowercase letter(s) indicate the nature of non-glycosidic groups (e.g., methyl, acetyl, or phenolic derivative moieties) that can be present on the substituents. Although relatively simple and practical to use, this abbreviated system lends itself to the naming of a large number of different combinations of structural building blocks and substituents. In its present state, this system is, therefore, adequate to name and differentiate all currently known complex oligosaccharides derived from heteroxylans and is sufficiently flexible to accommodate new structures as they become available.

Isotope labelling of proteins is important for progress in the field of structural proteomics. It enables the utilisation of the power of nuclear magnetic resonance spectroscopy (NMR) for the characterisation of the three-dimensional structures and corresponding dynamical features of proteins. The usual approach to obtain isotopically labelled protein molecules is by expressing the corresponding gene in bacterial or yeast host organisms, which grow on isotope-enriched media. This method has several drawbacks. Here, we demonstrate that it is possible to fully label a plant with (15)N-isotopes. The advantage of in vivo labelling of higher organisms is that all constituting proteins are labelled and become available as functional, post-translationally modified, correctly folded proteins. A hydroponics set-up was used to create the first example of a uniformly (15)N-labelled (> 98%) plant species, the potato plant (Solanum tuberosum L., cv. Elkana). Two plants were grown at low costs using potassium-[(15)N]-nitrate as the sole nitrogen source. At harvest time, a total of 3.6 kg of potato tubers and 1.6 kg of foliage, stolons and roots were collected, all of which were fully (15)N-labelled. Gram quantities of soluble (15)N-labelled proteins (composed mainly of the glycoprotein patatin and Kunitz-type protease inhibitors) were isolated from the tubers. NMR results on the complete proteome of potato sap and on an isolated protease inhibitor illustrate the success of the labelling procedure. The presented method of isotope labelling is easily modified to label other plants. Its envisioned impact in the field of structural proteomics of plants is discussed.

Water holding (WH) of soy protein gels was investigated to identify which length scales are most contributing to WH when centrifugal forces are applied. More specifically, it was attempted to differentiate between the contributions of submicron and supramicron length scales. MgSO4 and MgCl2 salt specificities on soy protein aggregation (submicron contribution) were used to create different gel morphologies (supramicron contribution). Obtained results showed that the micrometer length scale is the most important contribution to WH of gels under the applied deformation forces. WH of soy protein gels correlated negatively with Young's modulus and positively with recoverable energy. The occurrence of rupture events had only a limited impact on WH. The ease by which water may be removed from the gel, but not the total amount, seemed to be related to the initial building block size. These insights could be exploited in product development to predict and tune oral perception properties of (new) products.