The degradation of fats during thermophilic composting was investigated by adding lard of four different mixing ratios (0, 33.3, 42.9 and 50% on a dry weight basis) to dog food used as a model substrate for organic waste. The lard added at the mixing ratio of 33.3% did not inhibit the decomposition of organic matter in the dog food, with lard itself beginning decomposition after decay of more easily decomposable organic compounds of the dog food, 84 h from the start of composting. The percentage of lard decomposition reached as high as 29.3% by the end of 8 days of composting. By contrast, the decomposition of organic matter in the processed dog food was apparently inhibited when the portion of lard was greater than 33.3%, especially at the earliest stage of composting. It is possible, however, that lard would decompose vigorously once decomposition has begun, even when the ratio of lard is as high as 50%. The percentages of lard decomposition in composting mixtures with 42.9 and 50% lard were 15.7 and 9.50%, respectively, thus the higher the mixing ratio of lard, the lower the percentage of lard decomposition. However, it was found that the maximum decomposition rate of the lard was similar for all of the ratios tested; that is, approximately 5.0 x 10(-3) g carbon h(-1).
Agarase genes of non-marine agarolytic bacterium Cellvibrio sp. were cloned into Escherichia coli and one of the genes obtained using HindIII was sequenced. From nucleotide and putative amino acid sequences (713 aa, molecular mass; 78,771 Da) of the gene, designated as agarase AgaA, the gene was found to have closest homology to the Saccharophagus degradans (formerly, Microbulbifer degradans) 2-40 aga86 gene, belonging to glycoside hydrolase family 86 (GH86). The putative protein appears to be a non-secreted protein because of the absence of a signal sequence. The recombinant protein was purified with anion exchange and gel filtration columns after ammonium sulfate precipitation and the molecular mass (79 kDa) determined by SDS-PAGE and subsequent enzymography agreed with the estimated value, suggesting that the enzyme is monomeric. The optimal pH and temperature for enzymatic hydrolysis of agarose were 6.5 and 42.5ºC, and the enzyme was stable under 40ºC. LC-MS and NMR analyses revealed production of a neoagarobiose and a neoagarotetraose with a small amount of a neoagarohexaose during hydrolysis of agarose, indicating that the enzyme is a β-agarase.
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