PHYTASE ACTIVITY AND PHOSPHATE PARTITION DURING MALTING
نویسندگان
چکیده
منابع مشابه
Phytase activity in lichens
Phytase activity was investigated in 13 lichen species using a novel assay method. The work tested the hypothesis that phytase is a component of the suite of surface-bound lichen enzymes that hydrolyse simple organic forms of phosphorus (P) and nitrogen (N) deposited onto the thallus surface. Hydrolysis of inositol hexaphosphate (InsP6 , the substrate for phytase) and appearance of lower-order ...
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Phytate is the most abundant form of soil organic phosphorus (P). Increased P nutrition of arbuscular mycorrhizal plants derived from phytate has been repeatedly reported. Earlier studies assessed acid phosphatase rather than phytase as an indication of mycorrhizal fungi-mediated phytate use. We investigated the effect of mycorrhizal hyphae-mediated phytase activity on P uptake by maize. Two ma...
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Phytases are nutritionally important for increased bioavailability of dietary minerals and phosphate for monogastric animals including humans. Release of minerals and phosphate is accomplished by the enzymatic stepwise degradation of phytate (inositol hexaphosphate, IP6). Activity determinations of phytase is often based on analysis of total released phosphate (Pi), but phytase activity in its ...
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The changes in phytate, phytase activity and in vitro bioavailability of iron and zinc during soaking and germination of three white sorghum varieties (Sorghum bicolor L. Moench), named Dorado, Shandweel-6, and Giza-15 were investigated. Sorghum varieties were soaked for 20 h and germinated for 72 h after soaking for 20 h to reduce phytate content and increase iron and zinc in vitro bioavailabi...
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Ten Cryptococcus strains were screened for phytase activity, of which the Cryptococcus laurentii ABO 510 strain showed the highest level of activity. The cell wall-associated enzyme displayed temperature and pH optima of 62 degrees C and 5.0, respectively. The enzyme was thermostable at 70 degrees C, with a loss of 40% of its original activity after 3 h. The enzyme was active on a broad range o...
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ژورنال
عنوان ژورنال: Journal of the Institute of Brewing
سال: 1951
ISSN: 0046-9750
DOI: 10.1002/j.2050-0416.1951.tb01615.x