Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 407934
Title Enzyme-aided Fractionation of Brewer’s Spent Grains in Pilot Scale
Author(s) Forssell, P.; Treimo, J.; Eijsink, V.G.H.; Faulds, C.B.; Collins, S.; Schols, H.A.; Hinz, S.W.A.; Myllymaki, O.; Tamminen, T.; Zoldners, J.; Viljanen, K.; Waldron, K.W.; Buchert, J.
Source Journal of the American Society of Brewing Chemists 69 (2011)2. - ISSN 0361-0470 - p. 91 - 99.
DOI https://doi.org/10.1094/ASBCJ-2011-0408-01
Department(s) Food Chemistry Group
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) ferulic acid release - cell-wall components - antioxidant activity - humicola-insolens - hydrolysis - esterases - proteins - oligosaccharides - identification - solubilization
Abstract Brewer’s spent grain (BSG) is an important coproduct of the brewing industry and is generally used in animal feed. Recently, there has been considerable research into the use of enzymes to convert BSG into more value-added products. In this study, the efficiency of enzymatic fractionation of freshly produced BSG was studied in pilot scale. Carbohydrateand protein-degrading enzymes were applied sequentially to produce three fractions: carbohydrate hydrolysate, protein hydrolysate, and a solid lignin- carbohydrate residue. To minimize microbial contamination, processing was performed at 60°C for 4 hr. In all, 14 and 36% of the original dry matter was liberated by carbohydrase and protease, respectively. The carbohydrate- degrading enzyme cocktail produced cellulose- and hemicellulose- derived mono- and oligosaccharides. The protease treatment released peptide-enriched hydrolysate. Approximately half of the original BSG solids were solubilized during the two-stage enzymatic process. Although the protease efficiently released the majority of BSG proteins, the carbohydrate matrix was much less accessible to enzyme attack. The impact of scale-up to pilot scale was compared with previous laboratory-scale studies, and the results were found to be in good agreement.
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