| Literature DB >> 27516291 |
Wei Zou1, Mike Sissons2, Frederick J Warren3, Michael J Gidley3, Robert G Gilbert4.
Abstract
The roles that the compact structure and proteins in pasta play in retarding evolution of starch molecular structure during in vitro digestion are explored, using four types of cooked samples: whole pasta, pasta powder, semolina (with proteins) and extracted starch without proteins. These were subjected to in vitro digestion with porcine α-amylase, collecting samples at different times and characterizing the weight distribution of branched starch molecules using size-exclusion chromatography. Measurement of α-amylase activity showed that a protein (or proteins) from semolina or pasta powder interacted with α-amylase, causing reduced enzymatic activity and retarding digestion of branched starch molecules with hydrodynamic radius (Rh)<100nm; this protein(s) was susceptible to proteolysis. Thus the compact structure of pasta protects the starch and proteins in the interior of the whole pasta, reducing the enzymatic degradation of starch molecules, especially for molecules with Rh>100nm.Entities:
Keywords: Enzyme activity; GPC; Molecular structure; Pasta; Proteins; Starch
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Year: 2016 PMID: 27516291 DOI: 10.1016/j.carbpol.2016.06.016
Source DB: PubMed Journal: Carbohydr Polym ISSN: 0144-8617 Impact factor: 9.381