The aim of this applied research is to design a sustainable industrial scale enzyme based flax retting process. A systematic approach has been adopted. The screening and selection of enzymes for flax retting has been carried out. Alkaline pectinase has been identified as the most appropriate enzyme for the flax retting purpose. Optimisation of process parameters has been carried out using alkaline pectinase, non-ionic surfactants and chelating agents in terms of concentration of enzyme and other auxiliaries, time, temperature, liquid to solid ratio etc. Scale up experiments were performed. The BOD, COD and NKjeldahl of the process waste water have been evaluated. At the end, an eeconomical evaluation of the successful flax retting process has been performed. Paper for the 14th Autex World Textile Conference, May 26th-28th 2014, Bursa, Turkey.
MULTIFILE
Obesity and other lifestyle-related diseases are, amongst others, the result of an unbalanced diet and lifestyle. Excessive intake of energy, salt, saturated fat and sugar are leading to increased risk of chronic diseases, such as cardiovascular diseases, cancer and diabetes (WHO/FAO). Therefore, a healthier food intake (diet) is needed. But when is a food product healthier? From a nutritional perspective it is clear: the lower the levels of nutrients with a negative public health impact, the better the product fits in a healthy diet. However, when it comes to improving the health impact of the food supply through reformulation, other aspects are important as well. This article describes the ‘framework for product reformulation’, which integrates four essential disciplines: Nutrition & health, Foodtechnology, Legislation and Consumer perspective.
MULTIFILE
In the context of sustainability, the use of biocatalysis in organic synthesis is increasingly observed as an essential tool towards a modern and ‘green’ chemical industry. However, the lack of a diverse set of commercially available enzymes with a broad selectivity toward industrially-relevant substrates keeps hampering the widespread implementation of biocatalysis. Aminoverse B.V. aims to contribute to this challenge by developing enzymatic screening kits and identifying novel enzyme families with significant potential for biocatalysis. One of the most important, yet notoriously challenging reaction in organic synthesis is site-selective functionalization (e.g. hydroxylation) of inert C-H bonds. Interestingly, Fe(II)/α-ketoglutarate-dependent oxygenases (KGOs) have been found to perform C-H hydroxylation, as well as other oxyfunctionalization, spontaneously in nature. However, as KGOs are not commercially available, or even extensively studied in this context, their potential is not readily accessible to the chemical industry. This project aims to demonstrate the potential of KGOs in biocatalysis. In order to achieve this, the following challenges will be addressed: i) establishing an enzymatic screening methodology to study the activity and selectivity of recombinant KGOs towards industrially relevant substrates, ii) establishing analytical methods to characterize KGO-catalyzed substrate conversion and product formation. Eventually, the proof-of-principle demonstrated during this project will allow Aminoverse B.V. to develop a commercial biocatalysis kit comprised of KGO enzymes with a diverse activity profile, allowing their application in the sustainable production of either commodity, fine or speciality chemicals. The project consortium is composed of: i) Aminoverse B.V, a start-up company dedicated to facilitate chemical partners towards implementing biocatalysis in their chemical processes, and ii) Zuyd University, which will link Aminoverse B.V. with students and (bio)chemical professionals in creating a novel collaboration which will not only stimulate the development of (bio)chemical students, but also the translation of academic knowledge on KGOs towards a feasible biocatalytic application.
Proteins are nature-derived molecules that have found wide applications in biotechnology, pharmaceuticals and biocatalysis. A major limitation for the use of proteins in such applications is their lack of stability. This is due to the disruption of the tertiary structure of a protein, which is responsible for the function of a protein. Earlier studies have shown that three cysteine residues, which are strategically incorporated in the sequence, can be crosslinked with a tris-electrophile. This so-called in situ cyclization of proteins (INCYPRO) results in the rigidification of the protein structure and ultimately higher stability of the protein. For some proteins, it would be beneficial to use another amino acid residue for modification as cysteine residues can be important for the function of a protein, e.g. as disulfide bridges or as active sites residues. In this project, we will develop crosslinkers that are selective for methionine residues. Although these amino acids contribute to the function of proteins in biological systems, they are less important for the molecular function of proteins, thus making them suitable for crosslinking of proteins. Our plan is to first develop a set of trisfunctionalized crosslinkers that selectively react with the thioether functional group of methionine. Next, we will investigate the crosslinking conditions on the model protein (KIX domain) as a proof of concept. In the final step, we would like to prove that the function of the protein is retained by crosslinking the transpeptidase enzyme sortase A.
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