Publications by authors named "Kenneth Aase Kristoffersen"

Fourier transform infrared spectroscopy (FTIR) is a powerful analytical tool that has been used for protein and peptide characterization for decades. In the present study, the objective was to investigate if FTIR can be used to predict collagen content in hydrolyzed protein samples. All samples were obtained from enzymatic protein hydrolysis (EPH) of poultry by-products providing a span in collagen content from 0.

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A major challenge for successful cultured meat production is the requirement for large quantities of skeletal muscle satellite cells (MuSCs). Commercial microcarriers (MCs), such as Cytodex®1, enable extensive cell expansion by offering a large surface-to-volume ratio. However, the cell-dissociation step post cell expansion makes the cell expansion less efficient.

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Enzymatic protein hydrolysis (EPH) is an invaluable process to increase the value of food processing by-products. In the current work the aim was to study the role of standard thermal inactivation in collagen solubilization during EPH of poultry by-products. Hundred and eighty hydrolysates were produced using two proteases (stem Bromelain and Endocut-02) and two collagen-rich poultry by-products (turkey tendons and carcasses).

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A study of the effects of single and combined protease hydrolysis on myofibrillar versus collagenous proteins of poultry by-products has been conducted. The aim was to contribute with knowledge for increased value creation of all constituents of these complex by-products. A rational approach was implemented for selecting proteases exhibiting the most different activity towards the major protein-rich constituents of mechanically deboned chicken residue (MDCR).

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In this study we explore the potential of using Fourier-transform infrared (FTIR) spectra of trifluoroacetate-protein and peptide complexes for monitoring proteolytic reactions. The idea of treating dry-films of protein hydrolysates with trifluoroacetic acid (TFA) prior to FTIR analysis is based on the unique properties of TFA. By adding a large excess of TFA to protein hydrolysate samples, the possible protonation sites of the proteins and peptides will be saturated.

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Fourier-transform infrared (FTIR) spectroscopy was applied to predict the degree of hydrolysis (DH%) and weight-average molecular weight (M) in milk protein hydrolysates. Both DH% and M are important quality parameters of protein hydrolysates. Measuring these parameters and following their development during proteolytic reactions is therefore essential for process control and optimization in industry.

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In the presented study, Fourier-transform infrared (FTIR) spectroscopy is used to predict the average molecular weight of protein hydrolysates produced from protein-rich by-products from food industry using commercial enzymes. Enzymatic protein hydrolysis is a well-established method for production of protein-rich formulations, recognized for its potential to valorize food-processing by-products. The monitoring of such processes is still a significant challenge as the existing classical analytical methods are not easily applicable to industrial setups.

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The title compounds, [CdBr(CHNO)]·CHOH, (I), and [CdI(CHNO)], (II), are cadmium bromide and cadmium iodide complexes of the ligand ()-'-(pyridin-2-yl-methyl-ene)picolinohydrazide. Complex (I) crystallizes as the methanol monosolvate. In both compounds, the Cd cation is ligated by one O atom and two N atoms of the tridentate ligand, and by two bromide anions forming a BrNO penta-coordination sphere for (I), and by two iodide anions forming an INO penta-coordination sphere for (II), both with a distorted square-pyramidal geometry.

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In the title salt, [Zn(C(22)H(24)N(4)O)(CH(3)CN)][Zn(ClO(4))(C(22)H(24)N(4)O)(CH(3)CN)](ClO(4))(3), two differently coordinated zinc cations occur. In the first complex, the metal ion is coordinated by the N,N',N'',O-tetra-dentate acetamide ligand and an acetonitrile N atom, generating an approximate trigonal-bipyramidal coordination geometry, with the O atom in an equatorial site and the acetonitrile N atom in an axial site. In the second complex ion, a perchlorate ion is also bonded to the zinc ion, generating a distorted trans-ZnO(2)N(4) octa-hedron.

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