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  • 1
    Electronic Resource
    Electronic Resource
    Corn and potato α-1,4-glucan: α-1,4-glucan 6-glycosyltransferase. Evidence for separate hydrolytic and branching components (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 4330-4335 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00799a027
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of the potato α-1,4-glucan-α-1,4-glucan 6-glucosyltransferase (1968)
    s.l. : American Chemical Society
    Biochemistry 7 (1968), S. 3063-3072 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00849a006
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of an alkaline protease from the marine shipworm bacterium (1992)
    Springer
    Current microbiology 24 (1992), S. 111-117 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Bacterial isolates from the gland of Deshayes of the marine shipworm (Psiloteredo healdi) produced extracellular protease activity when cultured with 1% cellulose. A protease with a relative molecular mass of 36,000 daltons as determined by SDS-PAGE and a pI of 8.6 was isolated from the medium and purified to electrophoretic homogeneity. No carbohydrate appeared to be associated with the protein. The enzyme was activated and stabilized by relatively high salt concentrations (〉0.2M). Below 0.1M salt, significant protein aggregation occurred, as well as autohydrolysis of the protease, both of which resulted in the loss of activity. The specific activity of the enzyme was 65,840 proteolytic units/mg with azocasein substrate of optimal temperature (42°C), pH (9.0), and salt concentration (0.20M NaCl). The activity was stable up to 40°C, from pH 3.0 to pH 11.9, and from 0.1M to 3.5M NaCl. These stabilities, as well as the protease's stability in the presence of chelators, oxidizing agents, and heavy metals, suggest the enzyme has potential for use in relatively low temperature (40°C) industrial applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01570907
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  • 4
    Electronic Resource
    Electronic Resource
    Solution properites of dialdehyde starchPresented at the American Chemical Society meeting, Miami, Fla., April 7-12, 1957. (1959)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Polymer Science 35 (1959), S. 31-42 
    Details
    ISSN: 0022-3832
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Low levels of periodate oxidation increased the dispersibility of cornstarch in water at 98°C. Above the 10% level of oxidation, cornstarch became more resistant, and longer heating times were generally required to form stable solutions. Light-scattering, sedimentation, and viscosity measurements showed that the average particle weight in solutions of periodate-oxidized starches generally decreased with increased level of oxidation and time of heating. Introduction of dialdehyde groups into the anhydroglucose residues of the starch molecules thus made the structure labile toward degradation on heating in water. The experimental results showed, however, that an aggregation reaction also occurred in solutions of oxidized starches. This reaction was most evident at 10% oxidation level, but it was found to occur simultaneously with degradation over a range of oxidation levels. Aggregation probably results from the reaction of aldehyde groups of one molecule with hydroxyl groups of neighboring molecules. The observation that aggregation could be prevented by additon of glucose was explained by competition of hydroxyl groups of glucose with hydroxyl groups of starch in their reaction with aldehyde groups. The angular dependence of the light-scattering measurements indicated that formation of dumbbell-shaped particles by crosslinking of near-spherical particles was probably quite important to the aggregation reaction. Preliminary investigation of periodate-oxidized waxy maize starch showed that this starch had a much lower average molecular weight in solution than ordinary cornstarch at a comparable level of oxidation. This value may result from the contribution of amylose to the aggregation of ordinary oxystarch.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1959.1203512804
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  • 5
    Electronic Resource
    Electronic Resource
    Physical properties of periodate-oxidized amylose: Aggregation of oxidized amylose in aqueous solutions (1965)
    New York : Wiley-Blackwell
    Biopolymers 3 (1965), S. 497-508 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The ability of periodate-oxidized amylose to form aggregates in aqueous solution was studied by sedimentation, light scattering, and viscosity analyses. Ultracentrifuge schlieren patterns show that aggregation can be appreciable at pH 3.0 and 1.0. The hydroxyl ion-catalyzed degradation of the oxidized amylose is faster at pH 3.0 than at pH 1.0. Viscosity and sedimentation analyses conducted at pH 3.0 show that a minimum in the degree of aggregation of the oxidized molecules is obtained at 15-25% oxidation. Solubulity studies and x-ray diffraction patterns on retrograded amylose show that maximum solubility of the retrograded amylose is obtained by oxidizing to the extent of 25-35%. It was therefore concluded that in the general range of 20-30% periodate oxidation, the oxidized amylose has a minimum ability to form intermolecular hydrogen bonds. Outside of this range, oxidized amylose readily forms aggregates in aqueous solutions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1965.360030411
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  • 6
    Electronic Resource
    Electronic Resource
    A physical study of the degradation of periodate-oxidized amylose (1964)
    New York : Wiley-Blackwell
    Biopolymers 2 (1964), S. 327-335 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Changes in the viscosity of amylose that had been oxidized In an aqueous medium at pH 3.0 by sodium metaperiodate were followed as a function of time. Levels of 20, 40, 60, 80, and 100% periodate oxidation were attained. The rate of hydroxyl ion cleavage of the periodate oxidized amylose [(d1/[η]2)/dt = k] is proportional to the square of the degree of oxidation. That is, the hydroxyl ion hydrolysis of periodate oxyamylose occurs predominately at the site where two or more oxidized units exist side by side. A reaction mechanism is postulated to account for this slow breakdown of an isolated oxidized unit and for the fast degradation of two adjacent oxidized glucose; units. When two or more oxidized units exist side by side, the free aldehyde at carbon atom 3 is believed to be in equilibrium with a hydrate instead of a hemiacetal structure as in the case of a single, isolated, oxyglucose unit in amylose. The greater reversibility of the hydrate to the free aldehyde structure results in a greater possibility of β-alkoxycarbonyl elimination at sites where two or more oxidized glucose units exist side by side.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1964.360020404
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  • 7
    Electronic Resource
    Electronic Resource
    A microfibril-generating factor from the cellulase of Trichoderma reesei (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 321-327 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A combination of ionic strength reduction and diafiltration of Trichoderma reesei cellulate complex through a hollow fiber apparatus of 5000 molecular weight (MW) cutoff and subsequent passage of filtrate over a Spherogel-TSK 3000-SW column provided extracts that had the ability to generate microfibrils in filter paper and to disrupt filter paper and corn leaf tissue. Milligram quantities of material obtained from these extracts released small amounts of soluble carbohydrate from filter paper, required ferric iron for increased activity, and contained amino acids. Short fiber formation and disruption of filter paper during interaction with these extracts was enhanced by prior acid treatment and eliminated by prior base treatment. The amount of soluble carbohydrate hydrolyzed in 24 h from filter paper by whole cellulase complex was not changed by first disrupting the substrate with the extracts.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260310407
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