Naturally occurring antioxidants have gathered increased interest, not the least for their potential in promoting human health. The thermostable enzyme β-glucosidase B from the hyperthermophilic bacterium Thermotoga neapolitana has been successfully used for processing of antioxidative polyphenol glycosides in the development of environmentally friendly methods for extraction of antioxidants from agricultural waste. In a scientific study, the enzyme was effectively used in processing of onion waste through biocatalytic conversion (deglycosylation by hydrolysis) of quercetin glycosides to quercetin and hydrocarbons (Turner et al 2006 ).
Polyphenols and other secondary metabolites such as flavonoids occur naturally to large extent as glycosides which may make their detection difficult for example in food analysis but the β-glucosidase may be a useful catalyst for transforming these glycosides to a single measurable aglycone (see Figure). Besides having hydrolysis activity using water as acceptor, the enzyme can use alcohols as acceptors and thus has also great potential for chemical synthesis. The enzyme has been shown to be effective in catalyzing transglycosylations with hexanol and octanol as acceptor molecules and may be used for enzymatic production of alkyl glucosides, including eco-friendly surfactants with good biodegradability and low toxicity ( see Turner et al. 2007 ). Professor Eva Nordberg-Karlsson at Lund University in Sweden has led the research on the enzymatic characterisation of T. neopolitana β-glucosidase B and, in collaboration with the group of Prof. Derek T Logan (Dept. of Biochemistry and Structural Biology, Lund University), also determined the three-dimensional structure of the enzyme (Pozzo et al. 2010)
In cooperation with Dept. of Biotechnology at University of Lund in Sweden, the company Prokazyme is now offering the enzyme for sale for analytics and other small scale applications. The thermostable β-glucosidase B from Thermotoga neapolitana (product Bgl162, Beta-Glucosidase ) has many potential applications such as in antioxidant research and chemical synthesis.
Prokazyme, based in Reykjavik, Iceland, develops enzymes from the natural diversity of various extreme environments. Prokazyme mainly sells novel enzymes for research, diagnostic and industrial testing purposes through its website at www.prokazyme.com
Lund University is one of Sweden’s strongest research universities with more research funding awarded than any other Swedish full-scale university. Lund University was established as early as 1666 and the ranks among the 100 most influential Universities in the World. The Department of Biotechnology is one of the largest departments of the Chemical Institute at Lund University. The research activities include areas such as enzyme technology, microbial technology, industrial biotechnology, bioseparation and bioanalysis. The research focus of the group headed by Prof. Eva Nordberg Karlsson is within the area “enzymes of extremophilic microorganisms”, especially concerning thermostable glycoside hydrolases, and involve biochemical structure/function-related studies of enzymes with a biotechnological potential – www.biotek.lu.se