1988
DOI: 10.1271/bbb1961.52.2451
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Purification and some properties of water-soluble phospholipase B from Torulaspora delbrueckii.

Abstract: Water-soluble phospholipase B was purified to homogeneity from Torulaspora delbrueckii cell washings. The washings were concentrated by ultra filtration, and then a fraction with phospholipase B activity was precipitated with ammoniumsulfate, and purified by sequential column chromatographies on Octyl-Sepharose CL-4B, DEAE-Sephacel,and Sepharose 6B. The molecular weight of the enzyme was estimated to be 170,000~200,000 by SDS-polyacrylamide gel electrophoresis and by gel filtration with a Sephadex G-200 column… Show more

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Cited by 9 publications
(16 citation statements)
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“…5) One unit of enzyme activity was defined as the amount of enzyme needed to produce 1 mmol of free fatty acid per min at 30 C.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…5) One unit of enzyme activity was defined as the amount of enzyme needed to produce 1 mmol of free fatty acid per min at 30 C.…”
Section: Methodsmentioning
confidence: 99%
“…The enzyme solution was incubated with the above standard reaction mixture at 30 C, except that lysophosphatidylcholine (Lyso-PC) was used instead of PC. At appropriate intervals, the reaction products were extracted by the method of Bligh and Dyer.…”
Section: Methodsmentioning
confidence: 99%
“…Water-soluble phospholipase B activity was assayed by the method described previously 6 l The unit of activity is defined as the amount of enzyme which liberates I pmol of fatty acid per min from phosphatidylcholine at 30°C at two pHs (pH 2.5 and pH 7.5).…”
Section: Methodsmentioning
confidence: 99%
“…Recently, we isolated two types of phospholipase B, membrane-bound and water-soluble phospholipase B, from the yeast Toru/aspora deLbrueckii. 6 • 7 > Both types of enzymes were glycoproteins containing approximately 50% carbohydrate. These yeast phospholipase B were significantly activated at softening in storage, and were thought to be important in the autolysis process of yeast cells.…”
mentioning
confidence: 99%
“…Several PLB have been identified in various microorganisms (1)(2)(3)(4)(5)(6)(7)(8) and in plants (9) as well as in the brush border membrane of mature enterocytes from three animal species including guinea pig (10 -13), rat (14 -17), and rabbit (17,18). It was later found that intestinal PLB actually displays a broader substrate specificity, including diacylglycerol, monoacylglycerol (12), and retinyl esters (19).…”
mentioning
confidence: 99%