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Extraction, partial purification and characterization of proteases from the red seaweed Gracilaria edulis with similar cleavage sites on κ-casein as calf rennet
Journal article   Peer reviewed

Extraction, partial purification and characterization of proteases from the red seaweed Gracilaria edulis with similar cleavage sites on κ-casein as calf rennet

Ariestya Arlene Arbita, Nicholas A Paul, Julian Cox and Jian Zhao
Food Chemistry, Vol.330, pp.1-9
2020
PMID: 32569938
url
https://doi.org/10.1016/j.foodchem.2020.127324View
Published Version

Abstract

Caseinolytic activity Protease Cleavage site Milk-clotting Algae Gracilaria edulis
Enzymes currently used in cheesemaking have various drawbacks, and there is a continual need to find new coagulants. This study describes the extraction and biochemical characterization of two proteases from the red alga Gracilaria edulis. The proteases were extracted with phosphate buffer and partially purified by ammonium sulphate precipitation and dialysis. The enzymes exhibited optimum caseinolytic activity at 60 °C and a pH range of 6–8. They showed a high ratio of milk-clotting over caseinolytic activity, indicating they had an excellent milk-clotting ability. The proteases were confirmed to be serine protease and metalloprotease with molecular weight (MW) of 44 and 108 kDa. They exhibited high hydrolytic activity on κ-caseins, cleaving κ-casein at four main sites, one of which being the same as that of calf rennet, which is the first reported for an algal protease. The findings demonstrated that the proteases could potentially be used as a milk coagulant in cheesemaking.

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Domestic collaboration
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Web Of Science research areas
Chemistry, Applied
Food Science & Technology
Nutrition & Dietetics
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