Conversion and degradation of shellfish wastes by Serratia sp. TKU016 fermentation for the production of enzymes and bioactive materials

doi:10.1007/s10532-009-9303-x

機構典藏 > College of Sciences > Graduate Institute & Department of Chemistry > Journal Article > Item 987654321/61848

Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/61848

Title:	Conversion and degradation of shellfish wastes by Serratia sp. TKU016 fermentation for the production of enzymes and bioactive materials
Authors:	Wang, San-Lang;Chang, Tao-Jen;Liang, Tzu-Wen
Contributors:	淡江大學生命科學研究所
Keywords:	Antioxidant activity;Chitosanase;Protease;Serratia sp.;Shrimp shell wastes
Date:	2009-12
Issue Date:	2013-05-31 11:33:39 (UTC+8)
Publisher:	Dordrecht: Springer Netherlands
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.
Relation:	Biodegradation 21(3), pp.321-333
DOI:	10.1007/s10532-009-9303-x
Appears in Collections:	[Graduate Institute & Department of Chemistry] Journal Article

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