Digital standardization of lean manufacturing tools according to Industry 4.0 concept

Standardization is a key element in the effective use of lean manufacturing methodologies and tools for achieving process sustainability. Their combination is conducive to eliminating waste and improving the efficiency of production processes and guarantees the company that employees use the most efficient tools and do not waste time on unnecessary activities. These activities can be further improved by using digital solutions, in accordance with the concept of Industry 4.0. Therefore, the authors have developed the e-Lean system, whose task is to digitize selected lean manufacturing tools. The subject of this work is analysis of the functionality and effectiveness of the essential part of the e-Lean system in the form of specialized TPM (Total Productive Maintenance) software as an application. During implementation in a construction production company, the TPM application was tested by lean manufacturing and maintenance specialists. The research consisted of assessing the functionality and efficiency of processes in relation to conventional TPM solutions. Additional functionalities of the e-Lean system have been confirmed, such as systemic approval of machinery inspection, which requires passing all necessary steps at individual inspection points, direct access for supervisors to the results of inspection activities and their status, direct and easy access to photographic documentation of machines added during inspection both in optimization of working time and its course (e.g., the optimal number of steps taken by the employee during the inspection), as well as an efficient system of motivating employees (collecting points). The improvement in the effectiveness of processes was determined by measuring the control times for three control points (polymerization furnace, packing area, and defibering machines). The average control time was reduced from 16,200 to 13,923 s. Thus, thanks to the use of the application, it was found that the efficiency of using the TPM tool was increased by approx. 15% compared to previously used non-digital solutions.The authors are grateful to FCT (Fundação para a Ciência e Tecnologia, Portugal) who partially financially supported this work through the RD Units Project Scope UIDP/04077/2020 and UIDB/04077/2020

Membrane orientation of small multidrug resistance proteins

Oriëntatie eiwitten van de Small Multidrug Resistance familie in het membraan Het proefschrift van Mariska Kolbusz beschrijft de oriëntatie van eiwitten van de Small Multidrug Resistance (SMR) familie in het membraan en de correlatie tussen oriëntatie en de verdeling van positief geladen aminozuur residuen over de intra- en extracellulaire loops van de eiwitten. De ‘positive-inside’ regel stelt dat de meeste positief geladen residuen zich aan de cytoplasmatische kant bevinden en dat dit de oriëntatie bepaalt. De SMR-familie bevat twee typen eiwitten: ‘singles’ en ‘pairs’, die respectievelijk gecodeerd worden door een enkel gen of door een paar genen. Het EmrE-eiwit, een ‘single’, inserteert in het membraan in beide oriëntaties (zogenaamde ‘dual topology’). Om te bestuderen hoe representatief EmrE is voor de SMR eiwitten, bepaalde Kolbusz de oriëntatie van negen ‘singles’ en negen ‘pairs’ uit deze familie. Alle ‘singles’ inserteerden zoals EmrE met ‘dualtopology’. De analyse van de verdeling van de positief geladen residuen over de loops gaf aan dat er een goede correlatie met de oriëtatie was, maar er waren ook uitzonderingen. De twee eiwitten van de ‘pairs’ inserteerden weliswaar met een vaste oriëntatie, maar die was omgekeerd dan voorspeld door de positieve ladingsverdeling. Een gedetailleerde analyse van de rol van positief geladen residuen op de oriëntatie liet zien dat verschillende residuen de orientatie met verschillende sterkten beïnvloeden en dat andere, onbekende factoren de oriëntatie mede bepalen. Een genoom-analyse van negenentwintig Escherichia coli stammen toonde aan dat in tien stammen een langere versie van EmrE aanwezig is. De langere versie bevat vijf membraanspannende segmenten in plaats van vier en inserteert in één oriëntatie in het membraan in tegenstelling tot de normale versie. De functie van de lange versie is onbekend en moet verder onderzocht worden. The thesis of Magdalena Anna Kolbusz focuses on membrane orientation of members of the Small Multidrug Resistance (SMR) protein family and its correlation with distribution of positively charged amino acid residues over the membrane. As described in the positive-inside rule the positively charged residues are located mostly in cytoplasmic loops and seem to bethe key orientation determinant. In the SMR family there are two types of proteins: singlesandpairs encoded by single and paired genes respectively. The EmrE protein, which belongs to the singles, inserts into the membrane in two opposite orientations (dual topology). To verify the orientation of other SMR proteins membrane orientation of 9 singles and 9 pairs was established. It has been shown that singlesacquire dual topology as EmrE. Analysis of distribution of positively charged amino acids showed that there is a good correlation between the orientation and the distribution of positively charged residues, but also exceptions violating the positive-inside rule have been found. Among pairs, proteins inserted into the membrane in fixed, opposite orientations in agreement with the distribution of positively charged amino acids. A detailed analysis ofthe role of charged residues on orientation showed that different residues influence orientation with different strength and probably there are other factors involved in orientation determination. Analysis of 29 Escherichia colii strains revealed that in 10 strains a longer version of EmrE is present. The elongated protein contains 5 TMSs and acquires a single membrane orientation. Its function remains unknown and requires further research.

Transcriptome and exoproteome analysis of utilization of plant-derived biomass by Myceliophthora thermophila

Myceliophthora thermophila is a thermophilic fungus whose genome encodes a wide range of carbohydrate-active enzymes (CAZymes) involved in plant biomass degradation. Such enzymes have potential applications in turning different kinds of lignocellulosic feedstock into sugar precursors for biofuels and chemicals. The present study examined and compared the transcriptomes and exoproteomes of M. thermophila during cultivation on different types of complex biomass to gain insight into how its secreted enzymatic machinery varies with different sources of lignocellulose. In the transcriptome analysis three monocot (barley, oat, triticale) and three dicot (alfalfa, canola, flax) plants were used whereas in the proteome analysis additional substrates, i.e. wood and corn stover pulps, were included. A core set of 59 genes encoding CAZymes was up-regulated in response to both monocot and dicot straws, including nine polysaccharide monooxygenases and GH10, but not GH11, xylanases. Genes encoding additional xylanolytic enzymes were up-regulated during growth on monocot straws, while genes encoding additional pectinolytic enzymes were up-regulated in response to dicot biomass. Exoproteome analysis was generally consistent with the conclusions drawn from transcriptome analysis, but additional CAZymes that accumulated to high levels were identified. Despite the wide variety of biomass sources tested some CAZy family members were not expressed under any condition. The results of this study provide a comprehensive view from both transcriptome and exoproteome levels, of how M. thermophila responds to a wide range of biomass sources using its genomic resources.Peer reviewed: YesNRC publication: N