Kaisa Marjamaa / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Sara Kataja / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Mikko Arvas / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Natalia Maiorova / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Nina Aro / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Anu Koivula / VTT Technical Research Centre of Finland Ltd, Espoo, Finland
Topic: Novel Enzymes
β-glucosidases (BGL) have applications in hydrolysis and synthesis of oligosaccharides and various glycosides in food, beverage and lignocellulose processing, and production of pharma and cosmetic ingredients. Majority of BGLs belong to glycoside hydrolase (GH) families 1 or 3. In this paper we describe identification of secreted GH1 BGLs in transcriptomes of fungi and their cloning and heterologous expression in Trichoderma reesei. We have evaluated the thermal stability, end-product inhibition and substrate preference of these GH1 enzymes. The novel BGLs were remarkably tolerant towards end-product (glucose) inhibition when assayed on p-nitrophenyl β-D glucopyranoside as substrate. One of the enzymes, exhibiting ‘activation’ by glucose, high thermal stability and low activity in cellobiose hydrolysis, accepted pure aryl glycoside and various glycosides in hop extracts as substrates. This type of fungal BGLs might have potential in flavour modification in food and beverage processing.
