Hydrolysis Process Optimization and Functional Characterization of Yak Skin Gelatin Hydrolysates

Abstract

Yak (Bos grunniens) is an animal mainly living on the Tibetan Plateau. Yak skin is a valuable resource that is wasted in the meat production process. This study aimed to prepare yak skin gelatin hydrolysates (YSGH) from yak skin through enzymatic hydrolysis and investigate functional characterization of YSGH. We showed that trypsin was more effective than neutrase, papain, and pepsin in increasing the degree of hydrolysis (DH) of YSGH. The conditions of enzymatic hydrolysis were optimized using central composite design (CCD) and response surface method (RSM), and the highest DH value of 31.96% was obtained. We then analyzed the amino acid compositions and molecular weight distribution of peptides in YSGH. The obtained YSGH exhibited certain antioxidant activity and excellent ACE-inhibitory activity (IC50 = 0.991 mg/mL). In addition, the solubility (98.79%), emulsification, and foaming properties of YSGH developed here were also evaluated. With these physicochemical and biological functions, YSGH had potential applications in food, pharmaceuticals, and cosmetics as an ingredient.

Protein-Based 3D Biofabrication of Biomaterials

“…Gelatin, as the denatured collagen protein, is another common protein for 3D printing that has a similar composition to collagen. Gelatin cannot normally be found in nature and is obtained by partially hydrolyzing collagen, under the action of an enzyme such as neutrase [ 20 ] or under the action of an acid or an alkaline [ 21 ]. Keratin, abundant in feather, wool and hair, is another protein that can be classified into two different categories: alpha-types and beta-types [ 1 ].…”

Bovidae‐based gelatin: Extractions method, physicochemical and functional properties, applications, and future trends

“…Previously, Yang et al. (2019) extracted gelatin hydrolysate from yak skin and utilized enzymes neutrase, pepsin, trypsin, and papain. The hydrolysate recorded 97.78% of protein solubility, good emulsifying, and foaming ability, which makes it possible to be incorporated as a functional food ingredient.…”

Hybrid Gelatin Hydrogels in Nanomedicine Applications

“…25,26 As a polyampholyte, gelatin has both anionic and cationic hydrophobic groups obtained through different chemical modifications. 27,28 The chemical modification process can enhance the degree of protein cross-linking. The extent of cross-linking highly depends on the 3D structure and reactivity of the protein molecules, the quality of the modifying agent, and the composition and reactivity of the amino acid.…”

“…The advancement of functional proteins has increasingly evolved to achieve tailored biological properties, versatile functionality, and cost-effectivity in a precise and controlled fashion that can regulate their activities under recognizable conditions. , One of the most remarkable candidates of the functional protein is gelatin. Gelatin, derived from the collagen of skin, tendons, ligaments, and bones through hydrolysis or acidic or alkaline extraction, is a heterogeneous mixture of high-molecular-mass proteins with high water solubility that are absent in nature. , As a polyampholyte, gelatin has both anionic and cationic hydrophobic groups obtained through different chemical modifications. , The chemical modification process can enhance the degree of protein cross-linking. The extent of cross-linking highly depends on the 3D structure and reactivity of the protein molecules, the quality of the modifying agent, and the composition and reactivity of the amino acid .…”