The role of gender diversity on tax aggressiveness and corporate social responsibility: Evidence from Italian listed companies

The paper aims to examine the moderating role of gender diversity within a corporate board on the relationship between tax aggressiveness and a firm's corporate social responsibility (CSR) approach. This analysis was conducted using a set of indicators of financial statements of 168 Italian listed firms between 2011 and 2018. In addition, the sustainability reports of the same companies were observed. To perform the analysis a logit regression model is used. This paper shows different empirical results. First, this study notes that there is not a direct relationship between tax aggressiveness and CSR reporting. Second, gender diversity in a board of directors increases the orientation of companies to CSR disclosure, but does not have an impact on the relationship between tax aggressiveness and CSR disclosure. Instead, CEO gender has a positive influence on the relationship between corporate tax planning and CSR reporting in accordance with Global Reporting Initiative (GRI) standards. This study emphasizes the key role of gender diversity in the growth of the CSR approach and the reputation of companies. Therefore, governments and policymakers of major countries should promote gender diversity in corporate decision-making bodies, which contributes to achieving the Sustainable Development Goals (SDGs)

Dynamic surface behaviour of VPO catalysts under reactive and non-reactive gas compositions: an in-situ XAS study

The surface of an activated vanadium phosphorus oxide (VPO) catalyst was investigated by means of in situ X-ray absorption spectroscopy in the total electron yield mode. We observed significant changes of the V L3-near edge X-ray absorption fine structure (NEXAFS) when the material was transferred from room temperature to working conditions at 400°C in the reaction atmosphere. We studied the same VPO material under different gas compositions comprising the reaction mixture of n-butane and oxygen, pure oxygen and vacuum to elucidate the influence of the gas-surface interaction and the effect of the temperature. The results of this extensive study indicate a dynamic response of the catalyst surface to the applied conditions

Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex

Lipase activity found in the insoluble fraction of Araujia sericifera Brot. (Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications was assayed at different temperatures, pH values, and biocatalyst loads. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 °C. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under defined reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggests that this plant lipase is a promising biocatalyst for various biotechnological applications.Facultad de Ciencias Exacta

Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex

Lipase activity found in the insoluble fraction of Araujia sericifera Brot. (Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications was assayed at different temperatures, pH values, and biocatalyst loads. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 °C. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under defined reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggests that this plant lipase is a promising biocatalyst for various biotechnological applications.Facultad de Ciencias Exacta