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

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 degrees C, pH 6-7, <50 degrees C) and (pH 8-10, 40 degrees C, pH 5-10, <50 degrees 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.

journal_name

Biodegradation

journal_title

Biodegradation

authors

Wang SL,Chang TJ,Liang TW

doi

10.1007/s10532-009-9303-x

subject

Has Abstract

pub_date

2010-06-01 00:00:00

pages

321-33

issue

3

eissn

0923-9820

issn

1572-9729

journal_volume

21

pub_type

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