Goat milk yogurts were manufactured with the fortification of 2% (wt/vol) skim goat milk powder (SGMP), sodium caseinate (NaCn), whey protein concentrate (WPC), whey protein isolate (WPI), or yogurt texture improver (YTI). Yogurts were characterized based on compositional, microbiological, and textural properties; volatile flavor components (with gas chromatography); and sensory analyses during storage (21d at 5 °C). Compared with goat milk yogurt made by using SGMP, the other goat milk yogurt variants had higher protein content and lower acidity values. Goat milk yogurts with NaCn and WPC, in particular, had better physical characteristics. Using WPI caused the hardest structure in yogurt, leading to higher syneresis values. Acetaldehyde and ethanol formation increased with the incorporation of WPI, WPC, or YTI to yogurt milk. The tyrosine value especially was higher in the samples with NaCn and YTI than in the samples with WPC and WPI. Counts of Streptococcus thermophilus were higher than the counts of Lactobacillus delbrueckii ssp. bulgaricus, possibly due to a stimulatory effect of milk protein-based ingredients other than SGMP on the growth of S. thermophilus. Yogurt with NaCn was the best accepted among the yogurts. For the parameters used, milk protein-based products such as NaCn or WPC have promising features as suitable ingredients for goat milk yogurt manufacture.
BackgroundProteases can hydrolyze peptides in aqueous environments. This property has made proteases the most important industrial enzymes by taking up about 60% of the total enzyme market. Microorganisms are the main sources for industrial protease production due to their high yield and a wide range of biochemical properties. Several Aspergilli have the ability to produce a variety of proteases, but no comprehensive comparative study has been carried out on protease productivity in this genus so far.ResultsWe have performed a combined analysis of comparative genomics, proteomics and enzymology tests on seven Aspergillus species grown on wheat bran and sugar beet pulp. Putative proteases were identified by homology search and Pfam domains. These genes were then clusters based on orthology and extracellular proteases were identified by protein subcellular localization prediction. Proteomics was used to identify the secreted enzymes in the cultures, while protease essays with and without inhibitors were performed to determine the overall protease activity per protease class. All this data was then integrated to compare the protease productivities in Aspergilli.ConclusionsGenomes of Aspergillus species contain a similar proportion of protease encoding genes. According to comparative genomics, proteomics and enzymatic experiments serine proteases make up the largest group in the protease spectrum across the species. In general wheat bran gives higher induction of proteases than sugar beet pulp. Interesting differences of protease activity, extracellular enzyme spectrum composition, protein occurrence and abundance were identified for species. By combining in silico and wet-lab experiments, we present the intriguing variety of protease productivity in Aspergilli.Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-523) contains supplementary material, which is available to authorized users.
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