ESTIMATING SENSORY SHELF LIFE OF CHOCOLATE AND CARROT CUPCAKES USING ACCEPTANCE TESTS

This study determined the sensory shelf life of a commercial brand of chocolate and carrot cupcakes, aiming at increasing the current 120 days of shelf life to 180. Appearance, texture, flavor and overall quality of cakes stored at six different storage times were evaluated by 102 consumers. The data were analyzed by analysis of variance and linear regression. For both flavors, the texture presented a greater loss in acceptance during the storage period, showing an acceptance mean close to indifference on the hedonic scale at 120 days. Nevertheless, appearance, flavor and overall quality stayed acceptable up to 150 days. The end of shelf life was estimated at about 161 days for chocolate cakes and 150 days for carrot cakes. This study showed that the current 120 days of shelf life can be extended to 150 days for carrot cake and to 160 days for chocolate cake. However, the 180 days of shelf life desired by the company were not achieved. PRACTICAL APPLICATIONS This research shows the adequacy of using sensory acceptance tests to determine the shelf life of two food products (chocolate and carrot cupcakes). This practical application is useful because the precise determination of the shelf life of a food product is of vital importance for its commercial success. The maximum storage time should always be evaluated in the development or reformulation of new products, changes in packing or storage conditions. Once the physical-chemical and microbiological stability of a product is guaranteed, sensorial changes that could affect consumer acceptance will determine the end of the shelf life of a food product. Thus, the use of sensitive and reliable methods to estimate the sensory shelf life of a product is very important. Findings show the importance of determining the shelf life of each product separately and to avoid using the shelf time estimated for a specific product on other, similar products.

A Metal-Repressed Promoter From Gram-Positive Bacillus subtilis Is Highly Active and Metal-Induced in Gram-Negative Cupriavidus metallidurans

A synthetic version of the metal-regulated gene A (mrgA) promoter from Bacillus subtilis, which in this Gram-positive bacterium is negatively regulated by manganese, iron, cobalt, or copper turned out to promote high level of basal gene expression that is further enhanced by Co(II), Cd(II), Mn(II), Zn(II), Cu(II), or Ni(II), when cloned in the Gram-negative bacterium Cupriavidus metallidurans. Promoter activity was monitored by expression of the reporter gene coding for the enhanced green fluorescent protein (EGFP), and cellular intensity fluorescence was quantified by flow cytometry. Expression levels in C. metallidurans driven by the heterologous promoter, here called pan, ranged from 20- to 53-fold the expression level driven by the Escherichia coli lac promoter (which is constitutively expressed in C. metallidurans), whether in the absence or presence of metal ions, respectively. The pan promoter did also function in E. coli in a constitutive pattern, regardless of the presence of Mn(II) or Fe(II). In conclusion, the pan promoter proved to be a powerful tool to express heterologous proteins in Gram-negative bacteria, especially in C. metallidurans grown upon high levels of toxic metals, with potential applications in bioremediation. Biotechnol. Bioeng. 2010; 107: 469-477. (C) 2010 Wiley Periodicals, Inc.

Expression, Purification, Bioactivity, and Partial Characterization of a Recombinant Human Bone Morphogenetic Protein-7 Produced in Human 293T Cells

Bone morphogenetic protein-7 (BMP-7) is a secreted multifunctional growth factor of the TGF-beta superfamily, which is predominantly known for its osteoinductive properties and emerging potential for treatment of kidney diseases. The mature 34-38 kDa disulfide-linked homodimer protein plays a key role in the differentiation of mesenchymal cells into bone and cartilage. In this study, the full-length sequence of hBMP-7 was amplified and, then, cloned, expressed, and purified from the conditioned medium of 293T cells stably transfected with a lentiviral vector. The mature protein dimer form was properly secreted and recognized by anti-BMP-7 antibodies, and the protein was shown to be glycosilated by treatment with exoglycosidase, followed by western blotting. Moreover, the activity of the purified protein was demonstrated both in vitro, by alkaline phosphatase activity in C2C12 cells, and in vivo by induction of ectopic bone formation in Balb/c Nude mice after 21 days, respectively. This recombinant protein platform may be very useful for expression of different human cytokines and other proteins for medical applications.