𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Purification and characterization of the extracellular and cell-bound lipases from aPenicillium cyclopiumvariety

✍ Scribed by Danièle Druet; Najia Abbadi; Louis-Claude Comeau


Publisher
Springer
Year
1992
Tongue
English
Weight
404 KB
Volume
37
Category
Article
ISSN
1432-0614

No coin nor oath required. For personal study only.

✦ Synopsis


A new strain of Penicilfium cyclopium was f o u n d on m o u l d y G r e n o b l e walnuts. F r o m the culture filtrate, two new extracellular lipases (A-and B-lipase) were isolated and characterized. The mycelium contained one o f the two forms of lipase (B-lipase). The specificity of the cell-bound lipase linked to the mycelium was then studied. The enzyme was specific to shortchain h o m o g e n e o u s triacylglycerols; it preferred to attack the o-position rather t h a n the p -p o s i t i o n , and showed stereospecificity on the sn-1 position.


📜 SIMILAR VOLUMES


Purification and characterization of ext
✍ Véronique Planchot; Paul Colonna 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 699 KB

Extracellular alpha-amylase [(1 ~4)-a-D-glucan glucanohydrolase, EC 3.2.1.1] from Aspergillus fumigatus (Aspergillus sp. K-27) was purified to homogeneity by anion-exchange (DEAE-cellulose) and affinity (a-cyclodextrin-Sepharose) chromatography. The purified enzyme, a glycoprotein with 15% carbohydr

Purification and characterization of the
✍ R. Büttner; Dr. R. Bode; D. Birnbaum 📂 Article 📅 1987 🏛 John Wiley and Sons 🌐 English ⚖ 581 KB

The yeast Trichosporon adeninovorans secretes an amylase a t a high rate if grown in a medium containing starch or maltose. The enzyme was purified 29-fold by hydroxylapatite chromatography and gel filtration and characterized as a glucoamylase. The enzyme seems to be a glycoprotein with a molecular