H8510
Hesperidinase from Penicillium sp.
lyophilized powder, ≥10 units/g solid
Synonym(s):
Hesperidin-α-1,6-rhamnosidase
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About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
form
lyophilized powder
specific activity
≥10 units/g solid
storage temp.
2-8°C
Other Notes
Contains both α-L-rhamnosidase (EC 3.2.1.40) and β-D-glucosidase (3.2.1.21) activities.
Unit Definition
One unit will liberate 1.0 μmole of reducing sugar (as glucose) from hesperidin per min at pH 3.8 at 40 °C.
Physical form
Lyophilized powder containing sorbitol
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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L D Varbanets et al.
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 73(5), 9-15 (2011-12-15)
Investigation of 15 different glycoside activities of 64 strains isolated from water and invertebra of the Black Sea has shown that 64% of the studied strains displayed the capacity to synthesize enzymes with alpha-L-ramnosidase activity which varied from 0.01 to
Natalia Lorena Rojas et al.
Journal of industrial microbiology & biotechnology, 38(9), 1515-1522 (2011-01-12)
Rhamnosidases are enzymes that catalyze the hydrolysis of terminal nonreducing L-rhamnose for the bioconversion of natural or synthetic rhamnosides. They are of great significance in the current biotechnological area, with applications in food and pharmaceutical industrial processes. In this study
E V Gudzenko et al.
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 74(2), 14-21 (2012-06-13)
A scheme of isolation and purification of the enzyme with alpha-L-rhamnosidase activity has been developed. It included fractionation by ammonium sulfate and chromatography on TSK-gels Toyopearl HW-60, Fractogel TSK DEAE-650-s and Sepharose 6B. The enzyme was purified 60 times with
E V Hudzenko et al.
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 73(3), 46-53 (2011-08-04)
Influence ofsome technological parameters of cultivation ofproducers Cryptococcus albidus, Eupenicillinum erubescens, Bacillus sp. on the process of synthesis of extracellular enzyme alpha-L-rhamnosidase has been studied. The authors have determined optimal sources of carbon (0.2-0.3% rhamnose) and nitrogen (0.2% sodium nitrate
Lenka Weignerová et al.
Bioresource technology, 115, 222-227 (2011-09-06)
Extensive screening for a robust producer of α-L-rhamnosidase activity from well-defined strains of filamentous fungi, including multifactorial optimization (inducers, cultivation conditions) was accomplished. Enzyme production of the optimal producer Aspergillus terreus (non-toxigenic) was scaled up to 50L. α-L-Rhamnosidase, which was
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