Milk clotting and storage-tolerant peptidase from Aureobasidium leucospermi LB86

[Display omitted] •A. leucospermi peptidase meets the important requirements for cheese production.•Milk coagulation ability and low rates of proteolysis.•Long-term storage in a diluted form at 4 °C. Peptidases are widely used for softening meat, hydrolyzing protein, baking, cheese, and making wine....

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Bibliographic Details
Published in:Process biochemistry (1991) 2019-10, Vol.85, p.206-212
Main Authors: da Silva, Ronivaldo Rodrigues, Duffeck, Carlos Eduardo, Boscolo, Maurício, da Silva, Roberto, Gomes, Eleni
Format: Article
Language:English
Subjects:
Aluminum
Aureobasidium leucospermi
Baking
Biochemical characteristics
Biochemistry
Bioprocess
Carbon dioxide
Cheese
Clotting
Cobalt
Copper
Dairy products
Dithiothreitol
Enzymes
Exploration
Fungi
Iron
Meat
Mercury (metal)
Microorganisms
Milk
Organic chemistry
Peptidases
pH effects
Protease
Proteinase
Proteolysis
Serine
Serine peptidase
Solid-State fermentation
Storage
Wine
Yeast
Yeasts
Zinc
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Summary:[Display omitted] •A. leucospermi peptidase meets the important requirements for cheese production.•Milk coagulation ability and low rates of proteolysis.•Long-term storage in a diluted form at 4 °C. Peptidases are widely used for softening meat, hydrolyzing protein, baking, cheese, and making wine. A search for novel peptidases supports biotechnological innovation in the field of food chemistry. In general, microbial enzymes prospecting has mostly focused on filamentous fungi, and the potential of yeasts as enzyme producers has been little explored. This study focuses on a serine peptidase isolated from Aureobasidium leucospermi LB86. The purified enzyme was able to clot milk and, in storage assays, it maintained 90% of its activity for 40 days at 4 °C, and around 66% activity for 210 days. It had an estimated molecular mass of 33 kDa, highest activity at pH 7.0 and 45 °C, was stable in the pH range 5.5–9.0 at 4 °C and 25 °C, exhibiting activity higher than 75%, and retained 90% of activity at temperatures up to 45 °C for 120 min. Proteolytic activity increased in the presence of Ba2+ (18 ± 1.4%) and DTT (100 mM: 36 ± 5%), and was reduced by Co2+, Zn2+, Li+, Hg2+, Fe3+, Cu2+, Al3+, pepstatin A, and PMSF. These biochemical characteristics make this enzyme a promising candidate for use in cheesemaking.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2019.07.006