Enzymatic solubilization of brewers' spent grain by combined action of carbohydrases and peptidases

Janneke Treimo (Corresponding Author), Bjorge Westereng, Svein J. Horn, Pirkko Forssell, James A. Robertson, Craig B. Faulds, Keith W. Waldron, Johanna Buchert, Vincent G. H. Eijsink

Research output: Contribution to journalArticleScientificpeer-review

61 Citations (Scopus)

Abstract

Brewers’ spent grain (BSG), a high-volume coproduct from the brewing industry, primarily contains proteins, barley cell wall carbohydrates, and lignin. To create new possibilities for the exploitation of this large biomass stream, the solubilization of BSG by the combined action of carbohydrases (Depol 740 and Econase) and peptidase (Alcalase and Promod 439) was explored. Hydrolysis protocols were optimized with respect to temperature (influencing both microbial contamination and rate of enzymatic hydrolysis), pH, enzyme dose, order of enzyme addition, and processing time. On the basis of this approach, one- and two-step protocols are proposed taking 4−8 h and yielding combined or separate fractions of hydrolyzed oligosaccharides and liberated hydrolyzed protein. Optimized procedures resulted in the solubilization of >80% of the proteinaceous material, up to 39% of the total carbohydrates, and up to 42% of total dry matter in BSG. Of the original xylan present in BSG, 36% could be solubilized. Sequential and simultaneous treatments with the two enzyme types gave similar results. In sequential processes, the order of the carbohydrase and peptidase treatments had only minor effects on the outcome. Depol 740 released more pentoses than Econase and gave slightly higher overall dry matter solubilization yields.
Original languageEnglish
Pages (from-to)3316-3324
JournalJournal of Agricultural and Food Chemistry
Volume57
Issue number8
DOIs
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

Fingerprint

Dive into the research topics of 'Enzymatic solubilization of brewers' spent grain by combined action of carbohydrases and peptidases'. Together they form a unique fingerprint.

Cite this