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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 3 (1988), S. 175-178 
    ISSN: 1476-5535
    Keywords: Bacterial α-amylase ; Amyloglucosidase ; Starch hydrolysate ; Tapioca ; Lactobacillus plantarum ; Lactic acid fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Lactic acid production by an isolated ofLactobacillus plantarum was standardised on enzyme-hydrolysed tapioca (Manihot esculenta) flour, tapioca starch and soluble starch. Calculated yields of lactic acid (g from 100 g reducing sugars used) in nutrient media containing the abovementioned hydrolysates (10% reducing sugars) were 21.8%, 16.2% and 16.2%, respectively. Higher yields (29–34%) were obtained in media containing 5% reducing sugars. A conversion efficiency of 80–99% was achieved when the acid produced in the broth was neutralised periodically. One hundred milliliters of the medium (5% sugars) yielded 4.0–4.5 g of calcium lactate. These results indicate that unrefined starchy material can be successfully employed for the economic production of lactic acid. The same substrate can also be utilised for biomass production, as viable lactobacilli are being used for therapy in medicine.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 1 (1975), S. 173-181 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Aspergillus carbonarius produces exocellular pectinolytic enzymes which are active within the acid range of pH and therefore are useful in commercial processing of fruits. The fungus produces pectin methylesterase, a viscosity-reducing enzyme, and exo-polygalacturonase; but it does not produce transeliminases. The optimum pH range and temperature for the above-mentioned enzyme activities are 3.5 to 4.0 and 50°, respectively. Enzymic hydrolysates of both pectin and pectic acid contained only monogalacturonate. The enzymes are stable at pH 3.0 to 4.5 at room temperature (20–30°) for more than a month. A preliminary purification yielded two fractions, both of which showed viscosity-reducing as well as saccharogenic activities. Pectin methylesterase was unaffected when treated with 6M urea for 5 hr at pH 6.7 and 25°, whereas polygalacturonase and viscosityreducing activities were completely inactivated.
    Type of Medium: Electronic Resource
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