Physicochemical and Functional Properties of Yanbian Cattle Bone Gelatin Extracted Using Acid, Alkaline, and Enzymatic Hydrolysis Methods

Yanbian cattle, a high-quality indigenous breed in China, were selected due to their unique biological characteristics, underutilized bone byproducts, and potential as a halal-compliant gelatin source, addressing the growing demand for alternatives to conventional mammalian gelatin in Muslim-majority regions. This study investigates the physicochemical and functional properties of gelatin extracted from Yanbian cattle bones using three different methods: acid, alkaline, and papain enzymatic hydrolysis. The extraction yields and quality of gelatin were evaluated based on hydroxyproline content, gel strength, viscosity, amino acid composition, molecular weight distribution, and structural integrity. Specifically, A gelatin, prepared using 0.075 mol/L hydrochloric acid, achieved the highest yield (18.64%) among the acid-extraction methods. B gelatin, extracted with 0.1 mol/L sodium hydroxide, achieved the highest yield (21.06%) among the alkaline-extraction methods. E gelatin, obtained through papain hydrolysis, exhibited the highest yield (25.25%) among the enzymatic methods. Gelatin extracted via papain enzymatic hydrolysis not only retained better protein structure but also exhibited higher hydroxyproline content (19.13 g/100 g), gel strength (259 g), viscosity (521.67 cP), and superior thermal stability. Structural analyses conducted using SDS-PAGE, GPC, FTIR, XRD, and CD spectroscopy confirmed that papain extraction more effectively preserved the natural structure of collagen. Furthermore, amino acid composition analysis revealed that gelatin extracted via papain hydrolysis contained higher levels of essential residues, such as glycine, proline, and hydroxyproline, emphasizing the mild and efficient nature of enzymatic treatment. These findings suggest that, compared with acid and alkaline extraction methods, enzymatic hydrolysis has potential advantages in gelatin production. Yanbian cattle bone gelatin shows promise as an alternative source for halal gelatin production. This study also provides insights into optimizing gelatin production to enhance its functionality and sustainability.

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Publication Details

Journal
Gels
Published
2025-03-07
DOI
https://doi.org/10.3390/gels11030186
Citations
11
Primary Topic
Collagen: Extraction and Characterization
Type
article
Field-Weighted Citation Impact
6.57
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article

Physicochemical and Functional Properties of Yanbian Cattle Bone Gelatin Extracted Using Acid, Alkaline, and Enzymatic Hydrolysis Methods

Yin Lu, Guangjun Xia, Song Zhang, Hongyan Xu et al.
11 citations
Gels
Collagen: Extraction and Characterization
6.57
article

Physicochemical and Functional Properties of Yanbian Cattle Bone Gelatin Extracted Using Acid, Alkaline, and Enzymatic Hydrolysis Methods

Yin Lu, Guangjun Xia, Song Zhang, Hongyan Xu, Ruixuan Wang, Ziyi Jin, Duanduan Zhao
article en
11 citations

Abstract

Yanbian cattle, a high-quality indigenous breed in China, were selected due to their unique biological characteristics, underutilized bone byproducts, and potential as a halal-compliant gelatin source, addressing the growing demand for alternatives to conventional mammalian gelatin in Muslim-majority regions. This study investigates the physicochemical and functional properties of gelatin extracted from Yanbian cattle bones using three different methods: acid, alkaline, and papain enzymatic hydrolysis. The extraction yields and quality of gelatin were evaluated based on hydroxyproline content, gel strength, viscosity, amino acid composition, molecular weight distribution, and structural integrity. Specifically, A gelatin, prepared using 0.075 mol/L hydrochloric acid, achieved the highest yield (18.64%) among the acid-extraction methods. B gelatin, extracted with 0.1 mol/L sodium hydroxide, achieved the highest yield (21.06%) among the alkaline-extraction methods. E gelatin, obtained through papain hydrolysis, exhibited the highest yield (25.25%) among the enzymatic methods. Gelatin extracted via papain enzymatic hydrolysis not only retained better protein structure but also exhibited higher hydroxyproline content (19.13 g/100 g), gel strength (259 g), viscosity (521.67 cP), and superior thermal stability. Structural analyses conducted using SDS-PAGE, GPC, FTIR, XRD, and CD spectroscopy confirmed that papain extraction more effectively preserved the natural structure of collagen. Furthermore, amino acid composition analysis revealed that gelatin extracted via papain hydrolysis contained higher levels of essential residues, such as glycine, proline, and hydroxyproline, emphasizing the mild and efficient nature of enzymatic treatment. These findings suggest that, compared with acid and alkaline extraction methods, enzymatic hydrolysis has potential advantages in gelatin production. Yanbian cattle bone gelatin shows promise as an alternative source for halal gelatin production. This study also provides insights into optimizing gelatin production to enhance its functionality and sustainability.

GelsVol. 11(3)
Yanbian University (CN)
Openalex Percentile: Top 3%
Collagen: Extraction and Characterization
6.57
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