TY - JOUR A1 - Rade-Kukic, Koralja A1 - Schmitt, C. A1 - Rawel, Harshadrai Manilal T1 - Formation of conjugates between beta-lactoglobulin and allyl isothiocyanate effect on protein heat aggregation, foaming and emulsifying properties JF - Food hydrocolloids N2 - Whey proteins are widely used food ingredients due to their nutritional and functional properties (gelling, emulsifying, foaming). Owning to their structure (free thiol group, lysine residues, hydrophobic pocket), they can also be used as carriers for bioactives. In this study, conjugates between beta-lactoglobulin (beta-lg), and a bioactive metabolite from Brassicaceae vegetables, allyl isothiocyanate (AITC) were formed. Heat aggregation behavior (85 degrees C, 15 min), foaming and emulsifying properties of conjugates, at pH 4.0 and 7.1, were evaluated. Conjugates were formed by incubating beta-lg (0.5 mM) with AITC (0.05-20 mM) in water at pH 8.5 and room temperature. AITC primarily reacted with beta-lg's free thiol group (K-D = 0.2 +/- 0.1 mM) and thereafter with its amino groups (K-D 10.8 +/- 3.4 mM). AITC binding destabilized secondary and tertiary structure of beta-lg at pH 7.1, whereas induced molten globule conformation at pH 4.0. Conjugation reduced the heat aggregation of beta-lg at pH 7.1, while promoting it at pH 4.0. Conjugates adsorbed faster to air/water and oil/water interfaces at pH 4.0 than at pH 7.1. After 30 min, air/water surface tension was lower at pH 4.0 (47 mN m(-1)) than at pH 7.1 (57 mN m(-1)), while the surface tension of the oil/water interface was 8 mN m(-1) at both pHs. Foams produced with beta-lg-AITC conjugates at pH 4.0 exhibited higher volume and liquid stabilities compared to foams obtained at pH 7.1. Emulsions formed with conjugates at both pHs were destabilized by creaming due to flocculation, but coalescence was prevented. This study revealed that whey protein could potentially be used for the delivery of isothiocyanates in the form of foam or emulsion-based products. KW - beta-Lactoglobulin KW - Allyl isothiocyanate KW - Molecular structure KW - Heat aggregation KW - Foaming properties KW - Emulsifying properties Y1 - 2011 U6 - https://doi.org/10.1016/j.foodhyd.2010.08.018 SN - 0268-005X VL - 25 IS - 4 SP - 694 EP - 706 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Lamy, Elsa A1 - Rawel, Harshadrai Manilal A1 - Schweigert, Florian J. A1 - Capela e Silva, Fernando A1 - Ferreira, Ana A1 - Costa, Ana Rodrigues A1 - Antunes, Celia A1 - Almeida, Andre Martinho A1 - Coelho, Ana Varela A1 - Sales-Baptista, Elvira T1 - The effect of tannins on mediterranean ruminant ingestive behavior the role of the oral cavity JF - Molecules N2 - Sheep, cattle and goat are domestic ruminants of significant economic interest in the Mediterranean region. Although sharing the same pasture ranges, they ingest different plants and plant parts and, consequently different levels of tannins. This suggests an ability to detect and adapt ingestion according to animal physiological limits of tolerance for plant secondary metabolites. This review will detail the effects of dietary tannins on feeding behavior, and the role of the oral cavity in this process, with focus on such ruminant species. The role of salivary protein profile in tannin perception in the oral cavity, and as a defense mechanism, will be discussed. KW - polyphenols KW - diet selection KW - ruminants KW - salivary proteins KW - tannin-protein interaction Y1 - 2011 U6 - https://doi.org/10.3390/molecules16042766 SN - 1420-3049 VL - 16 IS - 4 SP - 2766 EP - 2784 PB - MDPI CY - Basel ER - TY - CHAP A1 - Khalil, Mahomound A1 - Isalm, K. Shaiful A1 - Raila, Jens A1 - Schenk, R. A1 - Rawel, Harshadrai Manilal A1 - Schweigert, Florian J. T1 - Content of lutein and lutein ester in tagetes and improvement of their stability T2 - Annals of nutrition & metabolism : journal of nutrition, metabolic diseases and dietetics ; an official journal of International Union of Nutritional Sciences (IUNS) KW - lutein ester KW - Emulsion KW - MCT oil KW - Stability KW - UV light Y1 - 2011 SN - 0250-6807 VL - 58 IS - 3 SP - 16 EP - 16 PB - Karger CY - Basel ER - TY - GEN A1 - Eggert, Kai A1 - Rawel, Harshadrai Manilal A1 - Pawelzik, Elke T1 - In vitro degradation of wheat gluten fractions by Fusarium graminearum proteases T2 - Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe N2 - Fusarium spp. infection of cereal grain is a common problem, which leads to a dramatic loss of grain quality. The aim of the present study was to investigate the effect of Fusarium infection on the wheat storage protein gluten and its fractions, the gliadins and glutenins, in an in vitro model system. Gluten proteins were digested by F. graminearum proteases for 2, 4, 8 and 24 h, separated by Osborne fractionation and characterised by chromatographic (RP-HPLC) and electrophoretic analysis (SDS-Page). Gluten digestion by F. graminearum proteases showed in comparison with gliadins a preference for the glutenins whereas the HMW subfraction was at most affected. In comparison with a untreated control, the HMW subfraction was degraded of about 97% after 4 h incubation with Fusarium proteases. Separate digestion of gliadin and glutenin underlined the preference for HMW-GS. Analogue to the observed change in the gluten composition, the yield of the proteins extracted changed. A higher amount of glutenin fragments was found in the gliadin extraction solution after digestion and could mask a gliadin destruction at the same time. This observation can contribute to explain the frequently reported reduced glutenin amount parallel to an increase in gliadin quantity after Fusarium infection in grains. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 877 KW - gluten KW - gliadin and glutenin fractions KW - peptides KW - serine and trypsin protease Y1 - 2020 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-435102 SN - 1866-8372 IS - 877 SP - 697 EP - 705 ER - TY - JOUR A1 - Eggert, Kai A1 - Rawel, Harshadrai Manilal A1 - Pawelzik, Elke T1 - In vitro degradation of wheat gluten fractions by Fusarium graminearum proteases JF - European food research and technology : official organ of the EuCheMS, Division of Food Chemistry N2 - Fusarium spp. infection of cereal grain is a common problem, which leads to a dramatic loss of grain quality. The aim of the present study was to investigate the effect of Fusarium infection on the wheat storage protein gluten and its fractions, the gliadins and glutenins, in an in vitro model system. Gluten proteins were digested by F. graminearum proteases for 2, 4, 8 and 24 h, separated by Osborne fractionation and characterised by chromatographic (RP-HPLC) and electrophoretic analysis (SDS-Page). Gluten digestion by F. graminearum proteases showed in comparison with gliadins a preference for the glutenins whereas the HMW subfraction was at most affected. In comparison with a untreated control, the HMW subfraction was degraded of about 97% after 4 h incubation with Fusarium proteases. Separate digestion of gliadin and glutenin underlined the preference for HMW-GS. Analogue to the observed change in the gluten composition, the yield of the proteins extracted changed. A higher amount of glutenin fragments was found in the gliadin extraction solution after digestion and could mask a gliadin destruction at the same time. This observation can contribute to explain the frequently reported reduced glutenin amount parallel to an increase in gliadin quantity after Fusarium infection in grains. KW - Gluten KW - Gliadin and glutenin fractions KW - Peptides KW - Serine and trypsin protease Y1 - 2011 U6 - https://doi.org/10.1007/s00217-011-1566-x SN - 1438-2377 VL - 233 IS - 4 SP - 697 EP - 705 PB - Springer CY - New York ER -