Conversion of shrimp shell by using Serratia sp. TKU017 fermentation for the production of enzymes and antioxidants.
A chitinase (CHT), and a protease (PRO) were purified from the culture supernatant of Serratia sp. TKU017 with shrimp shell as the sole carbon/nitrogen source. The molecular masses of CHT and PRO determined by SDS-PAGE were approximately 65 kDa and 53 kDa, respectively. CHT was inhibited by Mn2+, Cu2+ and PRO was inhibited by most tested divalent metals, EDTA. The optimum pH, optimum temperature, pH stability, and thermal stability of CHT and PRO were (pH 5, 50 degrees , pH 5 degrees ) and (pH 9, 40 degrees , pH 5 degrees ), respectively. PRO retained 95% of its protease activity in the presence of 0.5 mM SDS. The result demonstrates that PRO is SDS-resistant protease and probably has a rigid structure. The 4th day supernatant showed the strongest antioxidant activity (70%, DPPH scavenging ability) and the highest total phenolic content (196+/-6.2 microng of gallic acid equival/mL). Significant associations between the antioxidant potency and the total phenolic content, as well as between the antioxidant potency and free amino groups, were found for the supernatant. With this method, we have shown that shrimp shell wastes can be utilized and it's effective in the production of enzymes and antioxidants, facilitating its potential use in industrial applications and functional foods.
Wang
San-Lang
SL
Life Science Development Center, Tamkang University, Taipei 251, Taiwan. sabulo@mail.tku.edu.tw
Li
Jeng-Yu
JY
Liang
Tzu-Wen
TW
Hsieh
Jia-Lin
JL
Tseng
Wan-Nine
WN
D000818:Animals; D000975:Antioxidants / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003470:Culture Media / Q000378:metabolism; D004795:Enzyme Stability; D005285:Fermentation; D007218:Industrial Microbiology; D008970:Molecular Weight; D033542:Pandalidae; D010447:Peptide Hydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012037:Refuse Disposal / Q000379:methods*; D012705:Serratia / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism*; D013379:Substrate Specificity; D014866:Waste Products / Q000032:analysis
D000975:Antioxidants; D001426:Bacterial Proteins; D003470:Culture Media; D014866:Waste Products; D002688:Chitinases; D010447:Peptide Hydrolases