Preparation of diosgenin by the hydrolysis of rhizomes of dioscorea at a high temperature

1967 ◽  
Vol 1 (6) ◽  
pp. 334-335
Author(s):  
V. V. Panina ◽  
O. S. Madaeva
1997 ◽  
Vol 127 (3) ◽  
pp. 292-299 ◽  
Author(s):  
Yukiko Hanzawa ◽  
Daisuke Hiroishi ◽  
Chihiro Matsuura ◽  
Kenkichi Ishigure ◽  
Masashi Nagao ◽  
...  

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 367 ◽  
Author(s):  
Laura Sáez ◽  
Eoin Murphy ◽  
Richard J. FitzGerald ◽  
Phil Kelly

Tryptic hydrolysis of whey protein isolate under specific incubation conditions including a relatively high enzyme:substrate (E:S) ratio of 1:10 is known to preferentially hydrolyse β-lactoglobulin (β-LG), while retaining the other major whey protein fraction, i.e., α-lactalbumin (α-LA) mainly intact. An objective of the present work was to explore the effects of reducing E:S (1:10, 1:30, 1:50, 1:100) on the selective hydrolysis of β-LG by trypsin at pH 8.5 and 25 °C in a 5% (w/v) WPI solution during incubation periods ranging from 1 to 7 h. In addition, the use of a pilot-scale continuous high-temperature, short-time (HTST) heat exchanger with an extended holding time (EHT) of 5 min as a means of inactivating trypsin to terminate hydrolysis was compared with laboratory-based acidification to <pH 3 by the addition of HCl, and batch sample heating in a water bath at 85 °C. An E:S of 1:10 resulted in 100% and 30% of β-LG and α-LA hydrolysis, respectively, after 3 h, while an E:S reduction to 1:30 and 1:50 led >90% β-LG hydrolysis after respective incubation periods of 4 and 6 h, with <5% hydrolysis of α-LA in the case of 1:50. Continuous HTST-EHT treatment was shown to be an effective inactivation process allowing for the maintenance of substrate selectivity. However, HTST-EHT heating resulted in protein aggregation, which negatively impacts the downstream recovery of intact α-LA. An optimum E:S was determined to be 1:50, with an incubation time ranging from 3 h to 7 h leading to 90% β-LG hydrolysis and minimal degradation of α-LA. Alternative batch heating by means of a water bath to inactivate trypsin caused considerable digestion of α-LA, while acidification to <pH 3.0 restricted subsequent functional applications of the protein.


Weed Science ◽  
1970 ◽  
Vol 18 (5) ◽  
pp. 604-607 ◽  
Author(s):  
Roy Y. Yih ◽  
Colin Swithenbank ◽  
D. Harold McRae

Transformation of N-(1,1-dimethylpropynyl)-3,5-dichlorobenzamide (compound I) in soil occurs readily and two products are produced, initial cyclization giving 2-(3,5-dichlorophenyl)-4,4-dimethyl-5-methyleneoxazoline (compound II) followed by subsequent hydrolysis to N-(1,1-dimethylacetonyl)-3,5-dichlorobenzamide (compound III). These transformations can be brought aboutin vitro, the first step by means of acid or base, and the second by extended treatment with acid. The rate of cyclization and hydrolysis of compound I varies directly with soil temperature, being rapid at high temperature (37 C) and very slow at low temperature (5 C). The rate of chemical change of compound I in soil is influenced to a much greater degree by temperature than by soil moisture content. The effect of soil type on transformation of compound I was studied and compounds II and III were present in five of the six soils examined. The herbicidal activity of compounds II and III was negligible in comparison to compound I.


Polymer ◽  
1988 ◽  
Vol 29 (5) ◽  
pp. 860-870 ◽  
Author(s):  
Houchang Kheradmand ◽  
Jeanne François ◽  
Véronique Plazanet

2012 ◽  
Vol 39 ◽  
pp. 106-111 ◽  
Author(s):  
Yanhua Ma ◽  
Wenqi Ji ◽  
Xian Zhu ◽  
Ling Tian ◽  
Xueliang Wan

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