The effects of enzymatically aided acid‐swelling process on gelatin extracted from fish by‐products

Abstract

The objective of this study was to investigate the effects of the enzymatic aided acid‐swelling process on gelatin obtained from fish by‐products. For this purpose, gelatin was extracted by an acidic swelling procedure in the presence of protease extracted from Rainbow trout pyloric caeca. The yield of gelatin extraction and the most important physicochemical characteristics of the fish gelatin samples were investigated and compared with those of commercial bovine gelatin (CBG). The yields of gelatin from Epinephelus coioides skin (ESG) either with or without crude protease from pyloric caeca (15 units/g alkaline treated) were 14.98% and 50.89%, respectively. The yields of gelatin from Cyprinus carpio scales (CSG) with crude protease from pyloric caeca (15 units/g) were 49.97%. The gel strength of the CSG (259.66 g) was significantly higher than that of CBG (228.30 g) and ESG (187.75 g). Similarly, the gelling and melting points, foaming capacity and stability, and the SDS‐PAGE pattern of gelatins were compared. The electrophoretic pattern confirmed the results of gel strength which was due to the narrower alpha and beta bands in fish skin and commercial bovine gelatins than that of fish scales gelatin. The results of this research showed that the production of high‐quality gelatin can be achieved by the enzymatically aided acid‐swelling procedure from fish scales and skin.

An Integrated Approach for the Valorization of Sea Bass (Dicentrarchus labrax) Side Streams: Evaluation of Contaminants and Development of Antioxidant Protein Extracts by Pressurized Liquid Extraction

“…The SDS-PAGE technique is usually used to examine collagen or gelatin proteins obtained from fish skin. In this sense, the electrophoretic profiles of hoki and rainbow trout skin gelatin did not correspond to the profiles of the sea bass skin extracts [ 52 , 53 ]. MW of protein fragments of optimal sea bass tailfin extracts ranged between 8 and 80 kDa while those of the controls ranged between 8 and 141 kDa.…”

Enzyme Conditioning of Chicken Collagen and Taguchi Design of Experiments Enhancing the Yield and Quality of Prepared Gelatins

“…The Moosavi-Nasab method [ 60 ] with some modifications was used to determine the melting point; a solution of gelatin at the same concentration (6.67%) as after determination of gel strength and viscosity was used. A gelatin solution was introduced into a glass capillary of 3.0 mm in diameter to form a column at a height of 6.0 ± 1.0 mm.…”

Silica Gel Functionalized with Polyethylenimine as Advanced Sorbents for the Removal of Endotoxin from Gelatin

“…The gel strength of gelatin and ultralow endotoxin gelatin was determined on 6.67% (w/v) gelatin solution by a CT3 texture analyzer (Brookfield, USA) with a 1.27 cm-diameter flat-faced cylindrical plunger, using the Official Procedure of the Gelatin Manufacturers Institute of America, Inc. (GMIA). The hydroxyproline contents in gelatin were determined according to Moosavi-Nasab et al . The molecular weight distribution of gelatin samples was analyzed by high-performance liquid chromatography (HPLC, Shimadzu, Japan).…”