Xylan is one of the main non‐starch polysaccharides (NSPs) in cottonseed meal. This study aimed to evaluate the anti‐nutrition effect of xylan and to better understand cottonseed meal as a feed ingredient for the Chinese mitten crab, Eriocheir sinensis. A diet containing 280 g/kg fishmeal without cottonseed meal or xylan was formulated as a control (FM diet). A second diet (XYL diet) was supplemented with 53.3 g/kg xylan according to its amount in the third diet, the cottonseed meal diet (CSM diet), which was formulated to include 400 g/kg cottonseed meal. The last diet (CSM + XYLase diet) included 400 g/kg xylanase hydrolysed cottonseed meal, in which most xylan was hydrolysed. Diets were isonitrogenous (370 g/kg crude protein) and isoenergetic (17.58 KJ/g) and were randomly fed to 12 tanks of crabs for 8 weeks. Results showed that no difference was detected among groups in growth performance, serum biochemical index, or digestive and metabolism enzyme activity (p > 0.05). The apparent digestibility coefficient (ADC) of dry matter was FM > XYL > CSM + XYLase > CSM (p < 0.05). The ADC of protein in crab fed diet FM and XYL was significantly higher than CSM and CSM + XYLase (p < 0.05). Cottonseed meal decreased the fold height of the hindgut, upregulated the expression of peritrophin genes of Es‐PL44 and Es‐PP1 (p < 0.05), while xylan decreased the fold height of the hindgut and upregulated the expression of Es‐PP1 (p < 0.05). These results indicated that the negative effect of cottonseed meal and xylan on digestibility partly compensated by enhanced absorption of the hindgut innerly and by supplementation of xylanase externally, and cottonseed meal is an attractive alternative protein source in general for Chinese mitten crab.
Hormone-sensitive lipase (HSL) is an important regulator of cellular lipid homeostasis and catalyzes the hydrolysis of stored triacylglycerol. We identified and cloned for the first time the full-length cDNA sequence of HSL of the prawn Macrobrachium nipponense De Haan, 1849 [De Haan, 1833–1850] from a hepatopancreas cDNA library. The complete HSL sequence is 3,575 bp and encoded a 785 amino acid peptide with the catalytic core (GXSXG) containing a serine residue. The phylogenetic tree revealed that the gene of HSL of M. nipponense is closely related with that of Penaeus vanmameiBoone, 1931. The tissue distribution showed that the mRNA expression level of HSL in the hepatopancreas was significantly higher than that in other tissues (P < 0.05). Furthermore, the HSL expression in hepatopancreas was upregulated with the increase of dietary lipids but partially inhibited when the ratio of phospholipids was increased in the lipid mixture. These results demonstrate that HSL is involved in the lipid metabolism of M. nipponense and highlights the importance of phospholipids in lipid metabolism.
Hormone-sensitive lipase (HSL) is an important regulator of cellular lipid homeostasis and catalyzes the hydrolysis of stored triacylglycerol. In this study, the full-length cDNA sequence of HSL of Macrobrachium nipponense (M. nipponense) was identified and cloned for the first time from a hepatopancreas cDNA library by using reverse transcription-polymerase chain reaction and rapid amplification of cDNA ends. The complete HSL sequence was 3575 bp and encoded a 785 amino acid peptide with the catalytic core (GXSXG) containing a serine residue. The phylogenetic tree revealed that the gene of HSL of M. nipponense is closely related with that of Penaeus vanmamei. The tissue distribution showed that the mRNA expression level of HSL in the hepatopancreas were significantly higher than that in other tissues (P < 0.05). Furthermore, the quantitative real-time PCR results showed that HSL expression in the hepatopancreas was upregulated by an increase in dietary lipids and is partially inhibited when the ratio of phospholipids was increased in the lipid mixture. These results demonstrate that HSL is a novel gene involved in lipid metabolism of M. nipponensis and that HSL expression varies depending on the type of lipid.
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