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  • Chemistry  (3)
  • maize  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 410-413 
    ISSN: 1573-0972
    Keywords: Enterobacteriaceae ; fermentation ; lactic acid bacteria ; maize ; mawè ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lactic acid bacteria increased from 3.2 × 106 and 1.6 × 107 c.f.u./g (wet wt) to 2 × 109 and 1.6 × 109 c.f.u./g after 12 to 24 h of fermentation of home-produced mawè (a dough produced from dehulled maize) and commercial mawè, respectively. In commercial mawè, the yeast count increased from 1.3 × 105 to 2.5 × 107 c.f.u./g after 48 h of fermentation before decreasing, whereas in the home-produced mawè it increased from 2.5 × 104 to 3.2 × 107 c.f.u./g after 72 h of fermentation; the dominant yeasts were mainly Candida krusei, although C. kefyr, C. glabrata and Saccharomyces cerevisiae were also present. Enterobacteriaceae counts increased slightly during the initial stage ofthe fermentation, but decreased below the detection level after 24 to 48 h. Enterobacter cloacae was mostly found in commercial mawè and Escherichia coli mostly in homeproduced mawè.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 251-257 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Adsorption on crystalline cellulose of six endoglucanases (Endo I, II, III, IV, V and VI; 1, 4-β-D-glucan glucanohydrolase, EC 3.2.1.4) and two exoglucanases (Exo II and III; 1,4-β-D-glucan cellobiohydrolase, EC 3.2.1.92), purified from a commercial cellulase preparation of Trichoderma viride origin, was studied. Endo I, III, and V adsorbed strongly on Avicel cellulose, while adsorption of Endo II, IV, and VI was much lower. Also, the two exoglucanases could be divided into one enzyme (Exo III) that had a high adsorption affinity and another enzyme (Exo II) that adsorbed only moderately. Adsorption data fitted the Langmuir-type adsorption isotherm. However, adsorption was only partially reversible with respect to dilution. No relation could be found between adsorption affinity and degree of randomness in cellulose hydrolysis, measured as the diversity of released hydrolytic products. Kinetic measurements indicated that only part of the adsorbed enzyme molecules are hydrolytically active.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 160-167 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Six endoglucanases (Endo I, II, III, IV, V, and VI), three exoglucanases (Exo I, II, and III), and a β-glucosidase (β-gluc I) isolated from a commercial cellulase preparation of Trichoderma viride origin were examined as to their activities on xylan ex oat spelts. Endo I, II, and III as well as Exo II and III showed no activity toward xylan and were classified as specific glucanases. Less specificity was found for the endoglucanases Endo IV, V, and VI, Exo I, and β-gluc I, whose enzymes were able to hydrolyze xylan. With respect to product formation these xylanolytic cellulases fit the classification of xylanases generally accepted in the literature. Kinetic experiment with xylan, CM-cellulose, and p-nitrophenyl-β-D-glucoside revealed that Endo IV, V, an VI and Exo I prefer to hydrolyze β-1, 4-D-glucosidic linkages. β-Gluc I showed no clear substrate preference.
    Additional Material: 4 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 173-178 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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