The impact of supply chain agility on business performance in a high level customization environment

To improve business performance in rapidly changing environments, supply chain agility can be a crucial requisite to address responsiveness issues, especially in environments with high levels of customization. This paper examines the effect of supply chain agility on customer service, differentiation, and business performance. A survey research methodology was employed using a sample of 156 manufacturing firms that provide high levels of customization. In particular, structural equation modeling (SEM) was employed to evaluate the proposed model. The results suggest that supply chain agility influences customer service and differentiation positively. However, it does not affect business performance directly; instead, better business performance can be achieved and mediated through improved customer service and differentiation. In particular, differentiation through customer service is the most effective way to improve business performance, and supply chain agility can help to achieve high-level customer service. The paper advises managers on details of how to fulfil their business performance ambitions better through suggested key agile supply chain management activities

Pediatric urolithiasis: an 8-year experience of single centre

Objective The objective was to investigate the clinical features and metabolic and anatomic risk factors for kidney stone formation in our patient group

Purification, cloning, and overexpression of an alcohol dehydrogenase from Nocardia globerula reducing aliphatic ketones and bulky ketoesters

Parkot J, Gröger H, Hummel W. Purification, cloning, and overexpression of an alcohol dehydrogenase from Nocardia globerula reducing aliphatic ketones and bulky ketoesters. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 2010;86(6):1813-1820.For the huge amount of chiral chemicals and precursors that can potentially be produced by biocatalysis, there is a tremendous need of enzymes with new substrate spectra, higher enantioselectivity, and increased activity. In this paper, a highly active alcohol dehydrogenase is presented isolated from Nocardia globerula that shows a unique substrate spectrum toward different prochiral aliphatic ketones and bulky ketoesters as well as thioesters. For example, the enzyme reduced ethyl 4-chloro-3-oxo butanoate with an ee > 99% to (S)-4-chloro-3-hydroxy butanoate. Very interesting is also the fact that 3-oxobutanoic acid tert-butylthioester is reduced with 49.4% of the maximal activity while the corresponding tert-butyloxyester is not reduced at all. Furthermore, it has to be mentioned that acetophenone, a standard substrate for many known alcohol dehydrogenases, is not reduced by this enzyme. The enzyme was purified from wild-type N. globerula cells, and the corresponding 915-bp-long gene was determined, cloned, expressed in Escherichia coli, and applied in biotransformations. The N. globerula alcohol dehydrogenase is a tetramer of about 135 kDa in size as determined from gel filtration. Its sequence is related to several hypothetical 3-hydroxyacyl-CoA dehydrogenases whose sequences were derived by whole-genome sequencing from bacterial sources as well as known mammalian 3-hydroxyacyl-CoA dehydrogenases and -hydroxyacyl-CoA dehydrogenases from different clostridiae