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| Optimization of Conditions for Decolorization of Porcine Hemoglobin by Trypsin |
| YAO Lunhuan, HAO Gang, TANG Shanhu, LI Sining |
| College of Food Science and Technology, Southwest University for Nationalities, Chengdu 610041, China |
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Abstract This study comparatively evaluated the decolorization efficiency of porcine hemoglobin with trypsin and alkaline protease based on hydrolysis degree (DH), trichloroacetic acid (TCA) soluble nitrogen content and heme residue. Trypsin was determined to be more suitable for decolorizing porcine hemoglobin than alkaline protease. Using a fourfactor, three-level orthogonal array design, the optimal hydrolysis conditions for decolorizing porcine hemoglobin by trypsin were determined as follows: enzyme/substrate ratio 7 500 U/g, temperature 45 ℃, pH 7.5, and substrate concentration 8 g/100 mL. Under these conditions, the DH was 25.67%, and the TCA soluble nitrogen content, heme residue and total protein content of the peptide obtained powder were 80.05%, 18.34% and 83.17%, respectively. Molecular mass distribution analysis showed that small peptides with molecular masses less than 1 000 Da accounted for 94.20% of the peptide powder. TCA soluble nitrogen accounted for 96.25% of the protein content in the peptide powder, which is quite consistent with the results of molecular mass distribution.
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2020, Vol. 34 
