RESUMO
Tactile properties are one of the most important attributes of porous polymeric materials such as textiles, comprising a subjective evaluation index for textile materials and functional clothing, primarily affecting the sensation of comfort during the wearing of a garment. A new test method was proposed, and a mechanical measurement system was developed to objectively characterize the tactile properties of porous polymeric materials by simulating the dynamic contact processes during human skin contact with the materials and in consideration of different aspects of tactile sensations. The measurement system can measure the bending, compression, friction, and thermal transfer properties in one apparatus, and is capable of associating the objective measurements with the subjective tactile sensations. The test and evaluation method, the components of the mechanical measurement system, the definition and grading method of the evaluation indices, and the neural network prediction model from objective test results to subjective sensations of tactile properties were presented. The experiments were conducted for the objective tests and correlation tests. Seven types of porous polymeric sheet materials from seven categories for the tactile properties were cut to a size of 200 mm × 200 mm and tested. Each index of tactile properties was significantly different (P < 0.05) between different sheet materials. The correlations of bending, compression, friction, and thermal transfer properties with Kawabata KES test methods were analyzed. An intra-laboratory test was conducted and an analysis of the variance was performed to determine the critical differences of within laboratory precisions of the measurement system. This mechanical measurement system provides a method and system for objective measurement and evaluation of tactile properties of porous polymeric sheet materials in industrial application.
RESUMO
UNLABELLED: Deacetylation of 7-aminocephalosporanic acid (7-ACA) at position C-3 provides valuable starting material for producing semisynthetic ß-lactam antibiotics. However, few enzymes have been characterized in this process before now. Comparative analysis of the genome of the thermophilic bacterium Alicyclobacillus tengchongensis revealed a hypothetical protein (EstD1) with typical esterase features. The EstD1 protein was functionally cloned, expressed, and purified from Escherichia coli BL21(DE3). It indeed displayed esterase activity, with optimal activity at around 65°C and pH 8.5, with a preference for esters with short-chain acyl esters (C2 to C4). Sequence alignment revealed that EstD1 is an SGNH hydrolase with the putative catalytic triad Ser15, Asp191, and His194, which belongs to carbohydrate esterase family 12. EstD1 can hydrolyze acetate at the C-3 position of 7-aminocephalosporanic acid (7-ACA) to form deacetyl-7-ACA, which is an important starting material for producing semisynthetic ß-lactam antibiotics. EstD1 retained more than 50% of its initial activity when incubated at pH values ranging from 4 to 11 at 65°C for 1 h. To the best of our knowledge, this enzyme is a new SGNH hydrolase identified from thermophiles that is able to hydrolyze 7-ACA. IMPORTANCE: Deacetyl cephalosporins are highly valuable building blocks for the industrial production of various kinds of semisynthetic ß-lactam antibiotics. These compounds are derived mainly from 7-ACA, which is obtained by chemical or enzymatic processes from cephalosporin C. Enzymatic transformation of 7-ACA is the main method because of the adverse effects chemical deacylation brought to the environment. SGNH hydrolases are widely distributed in plants. However, the tools for identifying and characterizing SGNH hydrolases from bacteria, especially from thermophiles, are rather limited. Here, our work demonstrates that EstD1 belongs to the SGNH family and can hydrolyze acetate at the C-3 position of 7-ACA. Moreover, this study can enrich our understanding of the functions of these enzymes from this family.
