Obtaining durable enzyme powder via spray drying

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2005
Namaldı, Ayşegül
Serine alkaline protease (SAP, EC 3.4.21.62) produced by Bacillus species, that are the microbioreactors within the bioreactors, is one of the major industrial enzymes. In this study, after production by Recombinant Bacillus subtilis (BGSC-1A751), carrying pHV1431::subc gene in the complex media and separation of solids, SAP was dried by using a spray drier. Experiments were performed to investigate the stabilization of SAP during spray drying and subsequent storage. Initially, the effect of air inlet temperature of the spray drier on SAP activity was evaluated. For this purpose, SAP solutions were spray dried in the absence of any protective agents at five different air inlet temperature (700C, 900C, 1100C, 1200C, 1300C). As a result, increasing air inlet temperature lead to an increase in activity loss of SAP during drying. Thereafter, the effect of protective additives, glucose and maltodextrin (0.5%, 1%, 2% w/v), on SAP activity was investigated during spray drying. The activity loss of SAP was completely inhibited in the presence of glucose at 70, 90 and 1100C. However, the addition of maltodextrin was better than glucose for activity preservation of SAP at 1300C. Among the obtained results, 1% glucose addition was the best to preserve activity of SAP during spray drying. Then, structural change of SAP during drying was investigated. FTIR-ATR spectrum was used to evaluate the change in physical structure of the dried SAP powders in the presence of 1% glucose. From infrared images, at 900C more native-like structure for dried SAP powders was observed. In the last stage of this study storage stability of obtained SAP powders at 40C for a long period (6 months) was investigated. When considering all conditions, 0.5% maltodextrin addition was the best for stabilizing SAP powders along storage time.

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Citation Formats
A. Namaldı, “Obtaining durable enzyme powder via spray drying,” M.S. - Master of Science, Middle East Technical University, 2005.