JOURNAL OF COSMETIC SCIENCE 46 To date, the use of an 18 h incubation period for detecting the presence or absence of microbial contamination in a raw ingredient or personal care product formulation raw ingredient or personal care product formulation test sample by using an ATP biolumines- cence assay has not been reported elsewhere. There is no prior art to the best of our knowl- edge in using L-glutamic acid in an enrichment broth to promote the growth of mold in a rapid microbial detection method such as an ATP bioluminescence assay. ACKNOWLEDGMENTS We would like to thank Ly’ Tran-Osowski, Adele Bednar, and June Chen for their techni- cal assistance in conducting this study. REFERENCES (1 ) P. Meighhan, D. Nelson, K. Layte, and N. Foote, Rapid and reliable detection of molds within 24 hours. Poster No. Q037. American Society of Microbiology Conference 1997 (1997). (2 ) Evaluation, Validation and Implementation of Alternative and Rapid Microbiology Methods. Technical Report No. 33 (Parenteral Drug Association, Inc., Bethesda, MD, 2013). (3 ) Home & Beauty Solutions, Reagent technology-rapid detection, http://mycelsis.criver.com/Technical- Center/home-beauty-solutions/reagent-technology. (4 ) J. Madden, Screening raw material for microbial contamination. Pharm. Formul. Qual., (Oct. 46-5, 2005). (5 ) D. English and Y. Yang, Using an ATP bioluminescence assay to screen raw ingredients for microbial contamination. Cosmet. Toilet. Manuf. Worldw., 1, 25–28 (2005). (6 ) K. Willis, “ATP Bioluminescence and Its Use in Pharmaceutical Microbiology,” in Rapid Microbio- logical Methods, M. C. Easter. Ed. (Interpharm/CRC, New York, 2003), pp. 57–64. (7 ) L. Machlis, Factors affecting the lag phase of growth of fi lamentous fungus, Allomyces macrgynus. Am. J. Bot., 44, 113–119 (1957). (8 ) D. H. Griffi n, “Chemical Requirements for Growth,” in Fungal Physiology, 2nd Ed. (John Wiley & Sons, New York, 1996), pp. 130–157. (9 ) A. A. Ashtaputre and A. K. Shah, Studies on the exopolysaccharide from Sphingomonas paucimobilis-GS1: nutritional requirements and precursor-forming enzymes. Curr. Microbiol., 31, 234–238 (1995). (1 0) D. H. Griffi n, “Growth,” in Fungal Physiology, 2nd Ed. (John Wiley & Sons, New York, 1996), pp. 102–129. (1 1) K. W. Thomulka and A. G. Moat, Inorganic nitrogen assimilation in yeasts: alteration in enzyme ac- tivities associated with changes in culture conditions and growth phase. J. Bacteriol., 109, 25–33 (1972). (1 2) S. L. Tang and D. H. Howard, Uptake and utilization of glutamic acid by Cryptococcus albidus. J. Bacteriol., 115, 98–106 (1973). (1 3) C. F. Hirsch and J. C. Ensign, Nutritionally defi ned conditions for germination of Streptomyces viridochromogenes spores. J. Bacteriol., 126, 13–23 (1976). (1 4) S. A. Morse and T. A. Meitzner, “The Growth, Survival and Death of Microorganisms.” in Fundamentals of Microbiology. Jawetz, Melnick and Adelberg’s Medical Microbiology, 26 Ed., C. F. Brook, K. C. Carrol, J. S. Butel, S. A. Morse, and T. A. Mietzner. Eds. (McGraw Hill, New York, 2013), pp. 55–65. (1 5) G. Dorn and W. Rivera, Kinetics of fungal growth and phosphatase formation in Aspergillus nidulans. J. Bacteriol., 92, 1618–1622 (1996). (1 6) J. Shapira and K. Dittmer, Unsaturated amino acids. V. Microbiological properties of some halogenated olefi nic amino acids. J. Bacteriol., 82, 640–647 (1961). (1 7) A. Ogaswawara, K. Odahara, M. Tourne, T. Watanable, T. Mikami, and T. Matsumoto, Change in the respi- ration system of Candida albicans in the lag and log growth phase. Biol. Pharm. Bull., 29, 448–450 (2006). (1 8) S. Marin, V. Sanchis, R. Saenz, A. J. Ramos, I. Vinas, and N. Magan, Ecological determinants for ger- mination and growth of some Aspergillus and Penicillium spp. from maize grain. J. Appl. Microbiol., 84, 25–36 (1998).

J. Cosmet. Sci., 69, 47–56 ( January/February 2018) 47 Simulation of the Elastin and Fibrillin in Non-Irradiated or UVA Radiated Fibroblasts, and Direct Inhibition of Elastase or Matrix Metalloptoteinases Activity by Nicotinamide or Its Derivatives NEENA PHILIPS, JOVINNA CHALENSOUK-KHAOSAAT, and SALVADOR GONZALEZ, Department of Biology, Fairleigh Dickinson University, Teaneck, NJ (N.P., J.C-K.) and Department of Dermatology, Medicine and Medical Specialties, Alcala University, Madrid, Spain (S.G.). Accepted for publication November 28, 2017. Synopsis Skin aging/photoaging is associated with altered the structure of collagen and elastin fi bers, and in- creased activity of matrix metalloproteinases (MMP) and elastase. Nicotinamide and its derivatives, 2,6-dihydroxynicotinamide, 2,4,5,6-tetrahydroxynicotinamide, and 3-hydroxypicolinamide (collectively niacin derivatives) stimulate fi brillar collagen and heat shock proteins in dermal fi broblasts. The goal of this research was to extend the understanding of the anti–skin aging mechanism of these niacin derivatives through the stimulation of elastin (at the protein and promoter levels), fi brillin (1 and 2) in nonirradiated or ultraviolet (UVA) radiated dermal fi broblasts, and through the direct inhibition of MMP (1, 3, and 9) and elastase activities. UVA radiation stimulated elastin and inhibited fi brillin-1 and fi brillin-2 in dermal fi broblasts. The niacin derivatives signifi cantly stimulated the expression of elastin (transcriptionally), fi brillin-1 and fi brillin-2 in nonirradiated and UVA radiated fi broblasts, and directly inhibited MMP or elastase activity. Overall, the niacin derivatives, more so nicotinamide and 2,6-dihydroxynicotinamide, have anti–skin aging potential through the stimulation of elastin and fi brillin, and the direct inhibition of the extracellular matrix proteolytic enzymes. INTRODUCTION The structural integrity of the extracellular matrix (ECM), composed predominantly of collagen and elastin fi bers, is essential to skin structure and function (1–8). The structure of the ECM deteriorates with intrinsic aging, and exposure to environmental factors such as ultraviolet (UV) radiation (1–27). UVA radiation can penetrate the dermis and damage ECM through the generation of oxidative stress and infl ammation, and direct damage of biomolecules (9–14). The dermal fi broblasts are the primary synthesizers of the ECM proteins (1–4,8). Address all correspondence to Neena Philips at nphilips@fdu.edu and neenaphilips@optonline.net.