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摘要
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This study attempted to use fishery processing wastes to produce protease by Paenibacillus elgii
TKU051. Of the tested wastes, tuna head powder (THP) was found to be the most effective carbon and
nitrogen (C/N) source, and the optimal conditions were as follows: 0.811% THP, 0.052% K2HPO4
,
0.073% MgSO4
, initial pH of 8.96, incubation temperature of 31.4 ◦C, and incubation time of 3.092 days
to achieve the maximum protease activity of 2.635 ± 0.124 U/mL. A protease with a molecular weight
of 29 kDa was purified and biochemically characterized. Liquid chromatography with tandem mass
spectrometry analysis revealed an amino acid sequence of STVHYSTR of P. elgii TKU051 protease,
suggesting that the enzyme may belong to the M4 family of metalloproteases. The optimal activity
of the enzyme was achieved at 60 ◦C and pH 8. P. elgii TKU051 protease was strongly inhibited
by ethylenediaminetetraacetic acid and 1,10-phenanthroline, indicating its precise metalloprotease
property. P. elgii TKU051 protease displayed the activity toward casein and raw fishery wastes such
as tuna heads, tuna viscera, shrimp heads, and squid pens. Finally, the purified P. elgii TKU051
protease could improve the free-radical scavenging activity of fishery wastes. In short, P. elgii
TKU051 has potential application in eco-friendly approaches to efficiently convert fishery wastes to
metalloprotease. |
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