2013
DOI: 10.1016/j.foodres.2013.01.063
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Enzymatic hydrolysis of thermo-sensitive grape proteins by a yeast protease as revealed by a proteomic approach

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Cited by 19 publications
(15 citation statements)
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“…Most Saccharomyces cerevisiae strains show no extracellular protease activity on diagnostic agar media [16][17][18][19]69]. However, a 72 kDa extracellular pepsin-like aspartic protease was characterized from a PIR 1 strain [70,71]. The enzyme was active during grape juice fermentations, although it did not affect turbidity-inducing proteins, unless the wine was incubated at 38 • C for extended time.…”
Section: Microbial Proteasesmentioning
confidence: 99%
“…Most Saccharomyces cerevisiae strains show no extracellular protease activity on diagnostic agar media [16][17][18][19]69]. However, a 72 kDa extracellular pepsin-like aspartic protease was characterized from a PIR 1 strain [70,71]. The enzyme was active during grape juice fermentations, although it did not affect turbidity-inducing proteins, unless the wine was incubated at 38 • C for extended time.…”
Section: Microbial Proteasesmentioning
confidence: 99%
“…Yeast cell viability and protein secretion decrease after the first few months of the second fermentation in sparkling wine production (28), and after 9 months of aging typically no viable yeast cells remain (1). The further decrease in protein content we observed at 24 months is likely due to ongoing protein aggregation (31) or degradation by yeast enzymes (24,49,50 proteolytic activity by S. cerevisiae Pir1 (51). Surprisingly, even after extended aging on lees we only identified bona fide secreted yeast proteins, rather than intracellular proteins, suggesting that the impact of yeast autolysis on the aged sparkling wine proteome is not as extensive as previously thought.…”
Section: Discussionmentioning
confidence: 77%
“…The further decrease in protein content we observed at 24 months is likely due to ongoing protein aggregation (31) or degradation by yeast enzymes (24,49,50). For example, grape thaumatin-like proteins and chitinases are particularly susceptible to hydrolysis by proteolytic activity by S. cerevisiae Pir1 (51). Surprisingly, even after extended aging on lees we only identified bona fide secreted yeast proteins, rather than intracellular proteins, suggesting that the impact of yeast autolysis on the aged sparkling wine proteome is not as extensive as previously thought.…”
Section: Construction Of a Glycopeptide Ion Library -mentioning
confidence: 86%