Abstract
Leaf exudates from Aloe species, such as the Southern African Aloe ferox, are used in traditional medicines for both humans and livestock. This includes aloesin, a skin bleaching product that inhibits the synthesis of melanin. Aloesin, (a C-glycoside-5-methylchromone) can be released from aloeresin A, an ester of aloesin, through hydrolysis. The objective of the current study was to identify an enzymatic hydrolysis method for converting aloeresin A to aloesin, resulting in increased concentrations of aloesin in the aloe bitters extract. More than 70 commercially available hydrolytic enzymes were screened for the conversion of aloeresin A. An esterase (ESL001-02) from Diversa, a lipase (Novozym 388) and a protease (Aspergillus oryzae) preparation were identiWed during screening as being capable of providing conversion of pure aloeresin A, with the protease giving the best conversion (100%). It was found that a contaminating enzyme in Novo 388 was responsible for the conversion of aloeresin A to aloesin. This contaminating enzyme, possibly a protease, was able to give almost complete conversion using crude aloe bitters extract, doubling the concentration of aloesin in aloe bitters extract via the hydrolysis of aloeresin A. © Society for Industrial Microbiology and Biotechnology 2012.
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Steenkamp, L., Mathiba, K., Steenkamp, P., Phehane, V., Mitra, R., Heggie, S., & Brady, D. (2012). Biocatalytic conversion of aloeresin A to aloesin. Journal of Industrial Microbiology and Biotechnology, 39(7), 1091–1097. https://doi.org/10.1007/s10295-012-1101-5
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