Abstract
The packaging of abalone (H. squamata) (39.65 ± 0.24 mm TL) for long-term transportation (>8 hours) requires the addition of substances that provide an anesthetic effect so that it could reduce stress and maintain survival rate post transportation without having to repack. The objective was to investigate the expression pattern of HSP70 and HSP90 genes of abalone during transport with the addition of 2-phenoxyethanol. Abalone was packed using a styrofoam box with dimensions (42.5 x 75.5 x 27.5 cm3), containing 2 pcs of 10L Polyethylene (PE) plastic bags. The plastic bag consisted of 2 pcs of 25cm, 4-inch Polyvinyl Chloride (PVC) pipe for abalone attached. Both ends line enclosed with screen net and tied with rubber bands. Abalone density was 50 heads/pipe. Transportation tests were carried out using a dry system and wet system with and without the addition of 2-phenoxyethanol (PK, KK). Data analysis was done by paired sample ttest and ANOVA with a 95% confidence interval. The results showed that the best abalone survival (85%) was obtained in wet transport + 2-phenoxyethanol (PB) (p<0.05) within 24 hours of transportation.
Highlights
The tropical abalone Haliotis squamata is one of the indigenous gastropods along the southern coast of Bali, Jawa, and Sumatera
To find out whether the transportation test can induce HSP70 and HSP90, we investigated the temporal expression of HSP70 and HSP90 in haemolymph after transport assays
The graph showed that the activity of superoxide dismutase (SOD) was decreased after 6 h compared to the control until 24 hpt (Figure 3a)
Summary
The tropical abalone Haliotis squamata is one of the indigenous gastropods along the southern coast of Bali, Jawa, and Sumatera. This species is in great demand by consumers because it has similarities in shape and color to Taiwanese abalone tokobushi (H.diversicolor supertexta), which generally has a reddish round shell with a rough surface [1]. Stress on live transport can be caused by shocks, decreased oxygen levels, and high stock density causing organisms to respond by inducing a range of stress-responsible proteins, including chaperone molecules such as HSP70 and HSP90 [6]
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