Abstract
To investigate methods for improving the processing of porcine waste, porcine skin was hydrolyzed using different commercially available proteases (Alcalase, Flavorzyme, Neutrase, Bromeline, Protamex, and Papain) under several optimal conditions. Following enzymatic hydrolysis, the collagen hydrolysates (CHs) were fractionated by molecular weight (3 kDa) via membrane ultrafiltration. The CHs were analyzed for physical properties (pH, protein recovery, free amino group content, molecular weight distribution, and amino composition) as well as for functional properties (antioxidant activities and anti-aging activities). Among the CHs, CHs hydrolyzed by Alcalase (CH-Alcalase) exhibited the highest degree of hydrolysis compared to other CHs. Both “CH-Alcalase” and “CH-Alcalase < 3 kDa” fractions showed a considerably high antioxidant activity and collagenase inhibition activity. Therefore, resulting bioactives have potential for development as antioxidants and anti-aging ingredients in the food, cosmetics, and pharmaceuticals, from animal by-products.
Highlights
With increasing life expectancy, skin anti-aging procedures are receiving much attention
Results indicated that enzymatic hydrolysis by Alcalase clearly reduced the high MW of the control, and that ultrafiltration was an effective purification method that can be used to obtain low molecular weight peptides (
Various commercial proteases were tested for their potential usefulness in manufacturing proper collagen hydrolysates
Summary
Skin anti-aging procedures are receiving much attention. Collagen, used in skin care products as a cosmeceutical ingredient for anti-aging, is widely used in the cosmetic market. Livestock remains the main source of industrial collagen [1]. Large quantities of livestock by-products are discarded worldwide, as waste, by the food and meat processing industries. These may be utilized as important protein resources for novel food materials or converted to value-added products via hydrolysis, which is widely applied to improve and upgrade functional and nutritional properties of proteins [2,3]. Hydrolysis of collagen may play an important role in improving its bioavailability and suitability for use in various commercial processes
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