Conversion and degradation of shellfish wastes by <Emphasis Type="Italic">Serratia</Emphasis> sp. TKU016 fermentation for the production of enzymes and bioactive materials |
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Authors: | San-Lang Wang Tao-Jen Chang Tzu-Wen Liang |
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Institution: | (1) Graduate Institute of Life Sciences, Tamkang University, Taipei, 251, Taiwan;(2) Life Science Development Center, Tamkang University, Taipei, 251, Taiwan |
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Abstract: | A chitosanase and a protease were purified from the culture supernatant of Serratia sp. TKU016 with shrimp shell as the sole carbon/nitrogen source. The molecular masses of the chitosanase and protease determined
by SDS–PAGE were approximately 65 and 53 kDa, respectively. The chitosanase was inhibited completely by Mn2+, but the protease was enhanced by all of tested divalent metals. The optimum pH, optimum temperature, pH stability, and thermal
stability of the chitosanase and protease were (pH 7, 50°C, pH 6–7, <50°C) and (pH 8–10, 40°C, pH 5–10, <50°C), respectively.
SDS (2 mM) had stimulatory effect on TKU016 protease activity. The result demonstrates that TKU016 protease is SDS-resistant
protease and probably has a rigid structure. Besides, TKU016 culture supernatant (2% SPP) incubated for 2 days has the highest
antioxidant activity, the DPPH scavenging ability was about 76%. With this method, we have shown that shrimp shell wastes
can be utilized and it’s effective in the production of enzymes, antioxidants, peptide and reducing sugar, facilitating its
potential use in biological applications and functional foods. |
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