Corporate Social Responsibility in Family Firms: Status and Future Directions of a Research Field.

This systematic literature review contributes to the increasing interest regarding corporate social responsibility (CSR) in family firms-a research field that has developed considerably in the last few years. It now provides the opportunity to take a holistic view on the relationship dynamics-i.e., drivers, activities, outcomes, and contextual influences-of family firms with CSR, thus enabling a more coherent organization of current research and a sounder understanding of the phenomenon. To conceptualize the research field, we analyzed 122 peer-reviewed articles published in highly ranked journals identifying the main issues examined. The results clearly show a lack of research regarding CSR outcomes in family firms. Although considered increasingly crucial in family firm research, a study investigating family outcomes (e.g., family community status, family emotional well-being), as opposed to firm outcomes, is missing. This literature review outlines the current state of research and contributes to the actual debate on CSR in family firms by discussing how family firms can use CSR activities as strategic management tools. Moreover, our analysis shows a black box indicating how CSR links different antecedents and outcomes. The black box is significant since firms generally need to know where to allocate their scarce resources to generate the best outcomes. We identify nine research questions based on these findings, which we hope will inspire future research.

Probing enzyme promiscuity of SGNH hydrolases.

Several hydrolases of the SGNH superfamily, including the lipase SrLip from Streptomyces rimosus (Q93MW7), the acyl-CoA thioesterase I TesA from Pseudomonas aeruginosa (Q9HZY8) and the two lipolytic enzymes EstA (from P. aeruginosa, O33407) and EstP (from Pseudomonas putida, Q88QS0), were examined for promiscuity. These enzymes were tested against four chemically different classes of a total of 34 substrates known to be hydrolysed by esterases, thioesterases, lipases, phospholipases, Tweenases and proteases. Furthermore, they were also analysed with respect to their amino acid sequences and structural homology, and their phylogenetic relationship was determined. The Pseudomonas esterases EstA and EstP each have an N-terminal domain with catalytic activity together with a C-terminal autotransporter domain, and so the hybrid enzymes EstA(N)-EstP(C) and EstP(N)-EstA(C) were constructed by swapping the corresponding N- and C-terminal domains, and their hydrolytic activities were compared. Interestingly, substrate specificity and kinetic measurements indicated a significant influence of the autotransporter domains on the catalytic activities of these enzymes in solution. TesA, EstA and EstP were shown to function as esterases with different affinities and catalytic efficacies towards p-nitrophenyl butyrate. Of all the enzymes tested, only SrLip revealed lipase, phospholipase, esterase, thioesterase and Tweenase activities.