A Comparison of Sweet Cream Buttermilk Powder with Nonfat Dried Milk Solids in the Manufacture of Ice Cream

Properly dried sweet cream buttermilk, because of its high fat and lecithin contents, should make superior ice cream. Its use as a source of serum solids in ice cream. Its use as a source of serum solids in ice cream mix would open an outlet for this butter by-product and would serve the needs of ice cream manufacturers during nonfat dry milk solids shortage and it may make a higher score ice cream. The demand for milk solids shortage and it may make a higher score ice cream. The demand for milk solids has been increasing so rapidly that today the by-products of the dairy industry are being utilized as sources of human food to a much greater extent than before. In past years the greater bulk of creamery buttermilk has been utilized as animal feeds. Attempts are being made to convert more of this by-product into channels of human consumption. As the manufacture of sweet cream butter is increasing at a rapid pace, a larger supply of buttermilk product of high quality which is fit for human consumption is available in the market. Many previous investigators have used buttermilk products as a source of serum solids in ice cream mix with favorable results. The advantage claimed has been that it tends to improve the whipping ability of ice cream mixes and to impart richer flavor to the product. These beneficial qualities have been attributed to the butterfat and the phospholipids, of which lecithin is predominant. The work of Chapman and Supplee shows that buttermilk and cream contins several times as much licithin as skimmilk. The amounts of total phospholipids reported by Holm et al and Wright et al are approximately 1.77 per cent in dry buttermilk and 1.06 per cent in dry skim milk

Structure and Mechanism of Ergothionase from Treponema denticola

Ergothioneine is a sulfur-containing histidine derivative that emerges from microbial biosynthesis and enters the human body through intestinal uptake and regulated distribution into specific tissues. Although the proteins involved in biosynthesis and uptake are well characterized, less is known about the degradative pathways of ergothioneine. This report describes the crystal structure of the active form of ergothionase from the oral pathogen Treponema denticola complexed with the substrate analogue desmethyl-ergothioneine sulfonic acid. This enzyme catalyzes the 1,2-elimination of trimethylamine from ergothioneine and ergothioneine sulfonic acid by using a unique mode of substrate activation combined with acid/base catalysis. This structural and mechanistic investigation revealed four essential catalytic residues, which are strictly conserved in homologous proteins from common gastrointestinal bacteria and numerous pathogenic bacteria, suggesting that bacterial activity may play an important role in determining the availability of ergothioneine in healthy and diseased human tissue