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Digestibilities of the protein in various foods as determinedin vitro by an immobilized digestive enzyme assay (IDEA) (1989)

Thresher, Wayne C. ; Swaisgood, Harold E. ; Catignani, George L.

Springer

Plant foods for human nutrition 39 (1989), S. 59-65

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ISSN: 1573-9104

Keywords: immobilized digestive enzyme assay (IDEA) ; protein digestibility

Source: Springer Online Journal Archives 1860-2000

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition

Notes: Abstract The digestibility of the protein in various foods or food components was analyzed using an immobilized digestive enzyme assay (IDEA) system. The assay consists of two bioreactors, one containing pepsin and the other containing trypsin, chymotrypsin and intestinal mucosa peptidases. The fraction of the peptide bonds hydrolyzed during an extent of hydrolysis assay was correlated with independentin vivo determinations of the digestibilities. A correlation coefficient of 0.80 was obtained. The derived linear regression equation can be used to predict digestibility. The method is sensitive to structural modification of protein, as for example, those caused by effects of heat treatment.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01092402

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An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: Expression and bioselective adsorption of streptavidin-β-galactosidase (1994)

Walsh, Marie K. ; Swaisgood, Harold E.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 44 (1994), S. 1348-1354

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ISSN: 0006-3592

Keywords: streptavidin ; galactosidase ; fusion proteins ; plasmid vector ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Covalently immobilized biotin was used as a biospecific adsorbant to investigate the application of streptavidin as an affinity domain for simultaneous purification and immobilization of recombinant proteins. A streptavidin-β-galactosidase fusion protein was constructed and tested as a model system. The gene for streptavidin from Streptomyces avidinii was modified by polymerase chain reaction to mutate the stop codon and to facilitate cloning into an Escherichia coli expression vector yielding a versatile plasmid with 37 unique restriction enzyme sites at the 3' end. E. coli β-galactosidase was cloned in-frame to the streptavidin gene. Analysis of lysates of induced recombinant E. coli cells by SDS-PAGE and Western blots indicated that the 133.6-kDa fusion protein was expressed. Sulfosuccinimidyl-6-(biotinamido) hexanoate was covalently immobilized on 3-aminopropyl-controled-pore glass beads. Exposure of recombinant cell lysates to this support indicated that streptavidin-β-galactosidase was bioselectively adsorbed. The resulting biocatalyst contained 300 mg protein per gram of beads and exhibited a specific activity of 306 βmol/min per milligram protein with o-nitrophenyl-β-D-galactopyranoside as substrate corresponding to approximately 50% of that observed for commercially pure E. coli β-galactosidase. © 1994 John Wiley & Sons, Inc.

Additional Material: 4 Ill.