2000
DOI: 10.1002/1097-4660(200006)75:6<491::aid-jctb245>3.3.co;2-x
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Separation of the protease enzymes of Bacillus licheniformis from the fermentation medium by crossflow ultrafiltration

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Cited by 11 publications
(20 citation statements)
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“…The research activities related to the enzyme separations mostly report on the successive purification steps including ultrafiltration [18][19][20][21][22]. In our previous paper, we reported the recovery conditions of protease enzymes of Bacillus licheniformis from the fermentation medium in a crossflow ultrafiltration system [23]. However, none of the studies available in the literature on serine alkaline protease (SAP) reports the interaction of the enzyme with ultrafiltration membranes under the influences of different ions.…”
Section: Introductionmentioning
confidence: 99%
“…The research activities related to the enzyme separations mostly report on the successive purification steps including ultrafiltration [18][19][20][21][22]. In our previous paper, we reported the recovery conditions of protease enzymes of Bacillus licheniformis from the fermentation medium in a crossflow ultrafiltration system [23]. However, none of the studies available in the literature on serine alkaline protease (SAP) reports the interaction of the enzyme with ultrafiltration membranes under the influences of different ions.…”
Section: Introductionmentioning
confidence: 99%
“…Although membrane processes have many advantages, such as low energy consumption, no phase changes, easy scale-up, the fundamental problem of industrial membrane processes when compared with classic separation techniques is membrane fouling [1][2][3]. In order to solve this problem, many researchers have used membrane zeta potential as a key parameter [4][5][6][7][8], because membrane and particle zeta potentials provide important information about the nature and magnitude of membrane fouling caused by the membrane-particle interfacial interactions.…”
Section: Introductionmentioning
confidence: 84%
“…Protease activity was assayed spectrophotometrically using casein as substrate [13]. One unit of enzyme activity is defined as 4 nmol tyrosine released/min per ml.…”
Section: Enzyme Assaysmentioning
confidence: 99%