Aspartic Proteases in Food Industry

Nair, Indu C.; Jayachandran, K.

doi:10.1007/978-981-13-3263-0_3

Cited by 11 publications

(4 citation statements)

References 34 publications

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“…Aspartic proteases present well-established applications in the development of traditional and novel food products. They are also extensively used in cheese manufacturing (e.g., milk-clotting agents), beverage processing (e.g., clarification and preservation) [ 18 ], and in the pharmaceutical industry (e.g., in digestive aids and the treatment of certain lytic enzyme deficiency syndromes) [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

et al. 2022

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Microbial proteases, especially aspartic proteases, are an essential group of enzymes produced from different microorganisms. Microbial proteases have several applications, mainly in the food, beverage, cosmetic, and pharmaceutical industries, due to their efficiency in the processing and in the manufacturing stages. The yeast Rhodotorula mucilaginosa CBMAI 1528 was isolated from the Antarctic environment and was previously reported to have higher extracellular aspartic protease production. In addition, advances in the operational conditions of bioreactors for enzyme production are important to reduce the gap associated with scaling−up processes. This is the first study that evaluates the influence of oxygen transference (kLa) on the protease production of R. mucilaginosa yeast. To that end, batch cultures were created in a stirred tank bioreactor using Sabouraud dextrose broth at 25 °C for 72h under kLa values from 18 to 135 h−1. The results show that kLa (121 h−1) obtained at 500 rpm and 1.5 vvm plays an important role in protease production (124.9 U/mL) and productivity (6.784 U/L.h) as well as biomass (10.4 g/L), μmax (0.14 h−1) and Yx/s (0.484 g/g). In conclusion, R. mucilaginosa showed high yield production in aerobic culture with the efficiency of protease expression and secretion influenced by kLa. In this sense, our results could be used for further industrial investment.

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Section: Introductionmentioning

confidence: 99%

Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

et al. 2022

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“…An adequate RS is characterized by high specific hydrolytic activity and low general proteolytic activity 8 . In general, APs with milk clotting activity (MCA) meet both conditions, and are consequently favorite candidates in the search for RS 9 …”

Section: Introductionmentioning

confidence: 99%

“…In the Mediterranean basin, extracts from dried flowers of Cynara cardunculus L. are traditionally used to produce many varieties of sheep and goat cheeses. This coagulant produces cheeses with a soft texture, intense aroma, and slightly piquant flavor 9,10 . Natural variability of the plant extract concerning enzyme activity, as well as flower shortages, limit the use of C. cardunculus wildflower extract as an RS to artisanal production 4,11 .…”

Section: Introductionmentioning

confidence: 99%

Artichoke cv. Francés flower extract as a rennet substitute: effect on textural, microstructural, microbiological, antioxidant properties, and sensory acceptance of miniature cheeses

Colombo¹,

Cimino²,

Bruno

et al. 2020

J Sci Food Agric

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BACKGROUND The most common milk‐clotting enzymes in the cheese industry are recombinant chymosins. Food naturalness is a factor underpinning consumers' food choice. For consumers who avoid food with ingredients from genetically modified organisms (GMOs), the use of vegetable‐based rennet substitute in the cheese formulation may be a suitable solution. Artichokes that deviate from optimal products, when allowed to bloom due to flower protease composition, are excellent as raw material for vegetable rennet preparation. As enzymatic milk clotting exerts a significant impact on the characteristics of the final product, this product should be studied carefully. RESULTS Mature flowers from unharvested artichokes (Cynara scolymus cv. Francés) that did not meet aesthetic standards for commercialization were collected and used to prepare a flower extract. This extract, as a coagulant preparation, enabled the manufacture of cheeses with distinctive characteristics compared with cheeses prepared with chymosin. Rennet substitution did not affect the actual yield but led to significant changes in dry matter yield, humidity, water activity, protein content, and color, and conferred antioxidant activity to the cheeses. The rennet substitution promoted significant modifications in springiness, and in the microstructure of the cheese, with a more porous protein matrix and an increment in the size of the fat globules. Both formulations showed a similar microbiota evolution pattern with excellent microbiological quality and good sensory acceptance. CONCLUSIONS The rennet substitute studied here produced a cheese adapted to specific market segments that demand more natural and healthier products made with a commitment to the environment but well accepted by a general cheese consumer. © 2020 Society of Chemical Industry

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“…The major application of acid proteases is in cheese production in the dairy industry. Several species of fungi such as Aspergillus, Candida, Rhizomucor and Phanerochaete chrysosporium are reported to yield high amounts of aspartic protease enzymes while Aspergillus spp is the major producers for they possess several encoding genes such as pepA (Gomi et al, 1993;Nair & Jayachandran, 2019).…”

Section: Introductionmentioning

confidence: 99%

Cloning and Expression of an Active Aspartic Proteinase Gene From Aspergillus Oryzae DRDFS13 in Pichia Pastoris

Mamo¹,

Kostadinovska²,

Kangwa³

et al. 2020

Preprint

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BackgroundPichia pastoris is a yeast widely used in expressing recombinant proteins from eukaryotic organisms. In the present study, the total RNA was extracted from a eukaryotic fungus; Aspergillus oryzae DRDFS13 and reverse transcribed into cDNA using specific primers. The gene for aspartic protease was amplified and sequenced and then cloned into pGAPZαA for further expression in P. pastoris. The recombinant yeast (P. patoris X-33Ap) was cultivated in YPD media at pH 5 and 7 for 6 days and the production of recombinant proteins was checked by total protein determination, milk-clotting activity assay, and SDS-PAGE analysis. ResultsThe gene sequence results showed 98% similarity with aspartic protease gene from A. oryzae RIB40. The aspartic protease gene cloned into pGAPZαA (later pMKAP) was successfully expressed in P. pastoris as an active extracellular protease with the highest MCA (190.47 MCU/mL) of secreted enzyme from the recombinant yeast was obtained at pH 5 and 6 days of incubation time. The major protein expressed by the recombinant P. Pastoris X-33 AP has a molecular mass between 32 and 46 kDa. When analyzed for clotting activity, the protein was able to clot skim-milk in 2 min. The clotting activity was found to be 190.47 U/mL.ConclusionThus, the milk-clotting protease extracted form the recombinant yeast in the present study could be a suitable candidate for cheese production. However, further study of the recombinant proteins need to be carried out and its application in cheese production by analyzing the organoleptic and chemical properties of the cheese produced.

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Aspartic Proteases in Food Industry

Cited by 11 publications

References 34 publications

Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

Effects of Oxygen Transference on Protease Production by Rhodotorula mucilaginosa CBMAI 1528 in a Stirred Tank Bioreactor

Artichoke cv. Francés flower extract as a rennet substitute: effect on textural, microstructural, microbiological, antioxidant properties, and sensory acceptance of miniature cheeses

Cloning and Expression of an Active Aspartic Proteinase Gene From Aspergillus Oryzae DRDFS13 in Pichia Pastoris

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