@article{SaguTchewonpiNsoHomannetal.2015,
  author    = {Sagu Tchewonpi, Sorel and Nso, Emmanuel Jong and Homann, Thomas and Kapseu, Cesar and Rawel, Harshadrai Manilal},
  title     = {Extraction and purification of beta-amylase from stems of Abrus precatorius by three phase partitioning},
  series = {Food chemistry},
  volume    = {183},
  journal   = {Food chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0308-8146},
  doi       = {10.1016/j.foodchem.2015.03.028},
  pages     = {144 -- 153},
  year      = {2015},
  abstract  = {The stems of Abrus precatorius were used to extract a beta-amylase enriched fraction. A three phase partitioning method and a Doehlert design with 3 variables (ratio of crude extract/t-butanol, the ammonium sulphate saturation and pH) were used. The data was fitted in a second-order polynomial model and the parameters were optimized to enrich beta-amylase. Experimental responses for the modulation were recovery of activity and the purification factor. The optimal conditions were: a ratio of crude extract/t-butanol of 0.87 (v/v), saturation in ammonium sulphate of 49.46\% (w/v) and a pH of 5.2. An activity recovery of 156.2\% and a purification factor of 10.17 were found. The enriched enzyme was identified as a beta-amylase and its molecular weight was 60.1 kDa. K-m and V-max values were 79.37 mg/ml and 5.13 U/ml, respectively and the highest activity was registered at a temperature of 70 degrees C and a pH between 6 and 6.5. A significant stabilization of the beta-amylase was observed up to 65 degrees C. (C) 2015 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@article{ReinkensmeierBasslerSchlueteretal.2015,
  author    = {Reinkensmeier, Annika and Bassler, Sara and Schlueter, Oliver and Rohn, Sascha and Rawel, Harshadrai Manilal},
  title     = {Characterization of individual proteins in pea protein isolates and air classified samples},
  series = {Food research international},
  volume    = {76},
  journal   = {Food research international},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0963-9969},
  doi       = {10.1016/j.foodres.2015.05.009},
  pages     = {160 -- 167},
  year      = {2015},
  abstract  = {Generally, pea proteins are extracted at comparatively acidic or basic pH values to provide a basis for protein isolate production. Such processing steps result in partial denaturation of the proteins rendering them in most cases insoluble at food processing pH conditions and limiting their application in food products. Here, the comparison of the solubility properties of pea proteins in protein enriched fractions deriving from air classification is reported. Protein content, solubility, and physicochemical parameters of different fractions of the pea (Pisum sativum) variety 'Salamanca' were investigated as a function of pH using SDS-PAGE and surface hydrophobicity. Whole pea flour (20\% protein), air classified, protein-enriched pea flour (48\% protein), pea flour made from hulls (2.8\% protein), and pea protein isolate (81\% protein) served as test materials. Fractionation and pH value affected the composition and surface hydrophobicity of the proteins as well as the content of trypsin inhibitors. All samples showed a high buffering capacity in the range of pH 4 to 10. The direct comparison documents the comparatively better protein quality of the air classified, protein enriched pea fraction. The solubility of the pea protein isolate can be improved by using selected additives, giving new possibilities for plant protein application. Relevant technofunctional properties were determined and compared with two commercially available pea-based products (whole pea flour and an isolate). Water binding capacity was highest for the commercially available pea flour followed by the pea hull flour. Fat binding capacity remained more or less unchanged. (C) 2015 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@article{HuettlHettrichRiedeletal.2015,
  author    = {H{\"u}ttl, Christine and Hettrich, Cornelia and Riedel, Melanie and Henklein, Petra and Rawel, Harshadrai Manilal and Bier, Frank Fabian},
  title     = {Development of Peptidyl Lysine Dendrons: 1,3-Dipolar Cycloaddition for Peptide Coupling and Antibody Recognition},
  series = {Chemical biology \& drug design},
  volume    = {85},
  journal   = {Chemical biology \& drug design},
  number    = {5},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1747-0277},
  doi       = {10.1111/cbdd.12444},
  pages     = {565 -- 573},
  year      = {2015},
  abstract  = {A straightforward synthesis strategy to multimerize a peptide mimotopes for antibody B13-DE1 recognition is described based on lysine dendrons as multivalent scaffolds. Lysine dendrons that possess N-terminal alkyne residues at the periphery were quantitative functionalized with azido peptides using click chemistry. The solid-phase peptide synthesis (SPPS) allows preparing the peptide dendron in high purity and establishing the possibility of automation. The presented peptide dendron is a promising candidate as multivalent ligand and was used for antibody B13-DE1 recognition. The binding affinity increases with higher dendron generation without loss of specificity. The analysis of biospecific interaction between the synthesized peptide dendron and the antibody was done via surface plasmon resonance (SPR) technique. The presented results show a promising tool for investigations of antigen-antibody reactions.},
  language  = {en}
}
@article{BaierPurschkeSchmittetal.2015,
  author    = {Baier, Daniel and Purschke, Benedict and Schmitt, Christophe and Rawel, Harshadrai Manilal and Knorr, Dietrich},
  title     = {Effect of high pressure - low temperature treatments on structural characteristics of whey proteins and micellar caseins},
  series = {Food chemistry},
  volume    = {187},
  journal   = {Food chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0308-8146},
  doi       = {10.1016/j.foodchem.2015.04.049},
  pages     = {354 -- 363},
  year      = {2015},
  abstract  = {In this study, structural changes in micellar caseins and whey proteins due to high pressure - low temperature treatments (HPLT) were investigated and compared to changes caused by high pressure treatments at room temperature. Whey protein isolate (WPI) solutions as well as micellar casein (MC) dispersions and mixtures were treated at 500 MPa (pH 7.0 and 5.8) at room temperature, -15 degrees C and -35 degrees C. Surface hydrophobicity and accessible thiol groups remained nearly unchanged after HPLT treatments whereas HP treatments at room temperature caused an unfolding of the WPI, resulting in an increase in surface hydrophobicity and exposure of the thiol groups. For HPLT treatments, distinct changes in the secondary structure (increase in the amount of beta-sheets) were observed while the tertiary structure remained unchanged. Large flocs, stabilized by hydrophobic interactions and hydrogen bonds, were formed in casein containing samples due to HPLT treatments. Depending on the pH and the applied HPLT treatment parameters, these interactions differed significantly from the interactions determined in native micelles. (C) 2015 Elsevier Ltd. All rights reserved.},
  language  = {en}
}