The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries

Abstract

Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are classified in enzymes of class 3, the hydrolases, and the subclass 3.4, the peptide hydrolases or peptidase. Proteases are generally grouped into two main classes based on their site of action, that is, exopeptidases and endopeptidases. Protease has also been grouped into four classes based on their catalytic action: aspartic, cysteine, metallo, and serine proteases. However, lately, three new systems have been defined: the threonine-based proteasome system, the glutamate-glutamine system of eqolisin, and the serine-glutamate-aspartate system of sedolisin. Aspartic proteases (EC 3.4.23) are peptidases that display various activities and specificities. It has two aspartic acid residues (Asp32 and Asp215) within their active site which are useful for their catalytic activity. Most of the aspartic proteases display best enzyme activity at low pH (pH 3 to 4) and have isoelectric points in the pH range of 3 to 4.5. They are inhibited by pepstatin. The failure of the plant and animal proteases to meet the present global enzyme demand has directed to an increasing interest in microbial proteases. Microbial proteases are preferred over plant protease because they have most of the characteristics required for their biotechnological applications. Aspartic proteases are found in molds and yeasts but rarely in bacteria. Aspartic protease enzymes from microbial sources are mainly categorized into two groups: (i) the pepsin-like enzymes produced by Aspergillus, Penicillium, Rhizopus, and Neurospora and (ii) the rennin-like enzymes produced by Endothia and Mucor spp., such as Mucor miehei, M. pusillus, and Endothia parasitica. Aspartic proteases of microbial origin have a wide range of application in food and beverage industries. These include as milk-clotting enzyme for cheese manufacturing, degradation of protein turbidity complex in fruit juices and alcoholic liquors, and modifying wheat gluten in bread by proteolysis.

Combined ANN/EVOP Factorial Design Approach for Media Screening for Cost-effective Production of Alkaline Proteases from Rhizopus oryzae (SN5)/NCIM-1447 under SSF

“…The fungal proteases are active over a wide pH range (pH 4.0-11.0) and exhibit broad substrate specificity. They are also used in the pharmaceuticals, medical diagnosis and in the detergent industry as additives (Mamo and Assefa 2018). Fungal alkaline proteases are also used in food protein modification and processing (Neethu et al 2016).…”

Combined ANN/ EVOP Factorial Design Approach for Media Screening for Cost-effective Production of Alkaline Proteases from Rhizopus oryzae (SN5) / NCIM-1447 under SSF

“…The fungal proteases are active over a wide pH range (pH 4.0-11.0) and exhibit broad substrate specificity. They are also used in the pharmaceuticals, medical diagnosis and in the detergent industry as additives (Mamo and Assefa 2018). Fungal alkaline proteases are also used in food protein modification and processing (Neethu et al 2018).…”

Production, Optimization and Characterization of an Acid Protease From Filamentous Fungi by Solid-state Fermentation

“…Microbial acid proteases exhibit speci city against aromatic or bulky amino acid residues on both sides of the peptide bond, which is similar to pepsin, but their action is less stringent than that of pepsin (4).…”

“…Acid protease has a wide range of application in various industries to make a change in product taste, texture, and appearance and in waste recovery. Besides this, they have extensive applications in food industry, beverage industry, and pharmaceutical industry (4). The increasing importance of these enzymes and their numerous applications in different industries made us to investigate acid protease production from a new source.…”