Research Article Open Access

Understanding the Molecular Mechanisms of Proteases in Bioprocessing: A Review on the Future of the Food Industry

Abstract

Proteases are enzymes that break down proteins through peptide bond catalysis. A protease is a single polypeptide chain of some 250 amino acids and is devoid of sulfhydryl groups. The COOH-terminal tryptic peptide of the protease molecule contains some 43 residues. Because of this unique structure and mechanism, they play a crucial role in the bioprocessing industry, especially in food processing applications. Herein, the sources of proteases are discussed as plant-derived, animals-derived, and microbes-derived in the food processing industry, and each has certain unique characteristics: Plant-derived proteases exhibit alkaline pH optima, temperature stability, and lower allergenic potential, making them suitable for a range of food processing needs. Animal-derived proteases contribute to sensory effects in foods and exhibit versatility in functioning at extreme pH conditions and high or low temperatures. Microbes-derived proteases offer a wide pH range, thermostability, specificity and making them more valuable tools in food processing. Overall, the activity of proteases is influenced by several factors, including temperature, pH, substrate concentration, and the presence of inhibitors. Optimal protease activity is typically observed at alkaline pH and a temperature of around 37ºC. The enzyme activity increases with increasing substrate concentration until saturation is reached. The presence of inhibitors can affect protease activity, necessitating their removal for accurate measurement. Current research has shifted toward the development of engineered enzymes with enhanced properties for food processing. These engineered proteases can exhibit improved stability and activity under specific conditions, leading to enhanced efficiency and specificity in protein degradation. Such advancements hold great potential for enhancing food production processes.

Tuward J. Dweh, Neelanjana Choudhury*

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