Protein-peptide nutritional material prepared from surimi wash-water using immobilized chymotrypsin-trypsin.

BACKGROUND: In the production process of surimi, large quantities of wastewater are produced. Thus it would be interesting to develop an efficient protocol for the recovery of protein from hairtail surimi wash-water. RESULTS: A technique involving the use of immobilized chymotrypsin-trypsin (I-CT) was developed, providing a practical method for the preparation of protein-peptide nutritional material (PPNM). Under optimized reaction conditions, the recovery rate of nitrogen of surimi wash-water was measured as 98.3 ± 2.9%. Nutritional evaluation of the protein-peptide fraction demonstrated that it contained all essential amino acids (EAA) for humans, accounting for 44.1% of the total amino acid (TAA) content, which was determined to be 78.2 g per 100 g dry matter. The essential amino acid index (EAAI) and biological value (BV) were 101.7 (>95) and 76.7 respectively. A wide range of volatile flavor compounds (>50), including aldehydes, ketones, alcohols, hydrocarbons and heterocyclic compounds, were identified in PPNM by gas chromatography/mass spectrometry (GC/MS) analysis. CONCLUSION: An efficient and practical protocol for the recovery of protein from hairtail surimi wash-water has been developed. The PPNM prepared in this work could be used as a nutraceutical and as an ingredient of functional foods. © 2016 Society of Chemical Industry.

Changes of water state and gel characteristics of Hairtail (Trichiurus lepturus) surimi during thermal processing.

This study examined the changes of water state and gel characteristics of Hairtail surimi during thermal processing including two steps. The results showed that there were four content of water in Hairtail surimi gels. Water-holding capacity (WHC) and T23 relaxation time of water and gel strength increased from 47.01 to 78.97% and from 64.23 to 51.52 ms, respectively, and whiteness decreased from 63.87 to 55.22 during the entire thermal processing. Meanwhile, the texture properties including hardness, gumminess, and chewiness declined from 402.42 to 130.41 g, from 294.39 to103.70 g, and from 233.68 to 43.60 g, respectively, during the first step, and then increased markedly during the second step from 130.41 to 2,301.87 g, from 103.70 to 1,250.99 g, and from 43.60 to 978.51 g, respectively. Furthermore, the WHC and textural profile had positive correlation, and changes in protein secondary structure were interesting, with the α-helices decreasing significantly from 26.40 to 14.12%, while the ß-sheet and the random coil structure increasing significantly from 36.28 to 44.03%, and from 10.89 to 14.31%, respectively, and ß-turn structure increasing form 26.44 to 27.98% during the first step and then declining markedly during the second step, moreover ß-sheet had a fine positive correlation with WHC hardness and chewiness. Overall, dense, porous and compact three-dimensional network gel structure gradually formed. In a word, during thermal processing. WHC of Hairtail surimi increased, and protein secondary structure of protein became orderly, and a fine, dense gel formed during thermal processing. Water is considered as the highest and most important chemical constituent in surimi products. During surimi gelation, water molecules exist as bulk water and motionally restricted water on the protein surface. In order to gain more insights into the surimi heating-induced gelation processing, and improve the surimi gel properties, and give same advice to manufacturing enterprise, this work was conducted to study the structural changes of protein and water state during surimi gelation processing and performed along with the monitoring of the texture, WHC and other physical characteristics of surimi gel, as well as the microstructure of surimi gel.

Covalent immobilization of mixed proteases, trypsin and chymotrypsin, onto modified polyvinyl chloride microspheres.

A commercially available trypsin-chymotrypsin mixture was covalently immobilized onto modified polyvinyl chloride (PVC) microspheres, which were activated by the subsequent treatment of PVC microspheres with ethylenediamine and glutaraldehyde. The immobilized mixed protease was characterized by FT-IR and SEM analyses. Immobilization conditions were optimized by Box-Behnken design and the response surface method. The activity of the immobilized mixed protease prepared under optimal conditions (pH 6.6, 23 °C, 2 h) reached 1341 U/g. Compared with the free form, the immobilized enzyme possesses a slightly higher optimal pH value and a wider pH-activity profile, superior thermal stability, and a higher Km value. Reusability of the immobilized mixed protease indicated that >70% of the original activity was retained after having been recycled six times.