Novozymes wins P&G’s Supplier of the Year award for the third consecutive year

MONTREUX, SWITZERLAND – October 11, 2010 – Procter & Gamble (P&G), the largest consumer goods company in the world, recognizes Novozymes as one of its most outstanding suppliers.

Out of P&G’s 80,000 suppliers, Novozymes was one of 76 supplier and agency partners who were awarded an “Excellence Award.” Of those, Novozymes was one of only six companies recognized with the prestigious “Supplier of the Year” award. This was due to its strong commitment to innovation and supply excellence, which is a benchmark for the industry.
P&G announced the award winners during a celebration Thursday evening in connection with the 2010 Supplier and Agency Summit. This followed a P&G Supplier Award event at the 7th World Conference on Detergents which took place in Montreux, Switzerland, last week, where Novozymes was presented the Supplier of the Year trophy.

“We’re honored to win this award once again because it clearly shows that Novozymes’ customers value our commitment to developing innovative solutions. These awards indicate that we're delivering at a very high level and that our customers see us as partners and as instrumental to their business,” says Peder Holk Nielsen, Executive Vice President for Enzyme Business at Novozymes.

Since 2008, P&G has committed to meeting annually with its top-performing suppliers to recognize and celebrate those partners that have demonstrated their excellence in a number of categories associated with commercial, operational, innovation, and relationship performance. Novozymes has won the Supplier of the Year award every year since 2008.

Albufuse

Half-life extension through albumin fusion technology

A simple, single step expression platform for the production of proteins with extended half-life. Avoids post-production costs associated with chemical processing such as PEGylation.

Combine albumin fusion albufuse with our yeast expression technology and cGMP/Q7-manufacturing services to maximize the benefits of working with us.

Key benefits

• Increased half-life of the active molecule, resulting in:
  • Less frequent administration
  • Increased bioavailability therefore lowered dosage
• Fewer side effects with improved tolerance
• Competitive production costs
• Specific albumin fusion binding matrices available for improved downstream purification
• Animal-free
• Genetically fused.

Application areas

• Protein drug half-life extension and delivery technologies
• Protein expression.

Recombumin

The future of formulation is clear!

The world’s first and only, animal-free, commercially available recombinant human albumin, approved for use in the manufacture of human therapeutics.

Used in the manufacture of the FDA and EMEA approved M-M-R™ II childhood vaccine from Merck and Co., Recombumin* is also being evaluated as an excipient, or ingredient, in several other products undergoing clinical development in the US and EU. 

Key benefits

• Stabilize your product in liquid formulation at room temperature
• Improve visual appearance of lyophilized product and decrease dissolution time
• Manufactured to Q7 GMP in FDA, Health Canada and MHRA inspected facilities
• Extend product bioavailability
• Half-life extension of peptides.

Application areas

• Protein and peptide drug formulation
• Vaccine formulation
• Drug manufacturing ingredient
• Drug targeting and delivery.

Albumin 'Key Points'

What is albumin?

Albumin is an important intravascular and extravascular protein; it contributes strongly to the maintenance of colloid osmotic pressure.

Why is it important?

Binding and transport, osmotic pressure, free radical scavenging, platelet function inhibition and antithrombotic effects.

What causes serum albumin to decrease?

Decreased synthesis, increased catabolism, increased loss & redistribution.

* Consequences of decreased plasma albumin

1. Decreased ligand binding.

2. Decreased plasma colliod pressure

* Disease processes associated with Hypoalbuminaemia

In critical illness, there is a stronger correlation between colloid oncotic pressure and Total protein than with albumin.

Albumin decreases in burns, liver disease, renal disease, pre-eclampsia, stress and sepsis.

* Albumin as a prognostic index

Serum albumin concentration in critical illness is inversely related to the risk of death.

* Correcting Hypoalbuminaemia

The "normalisation" of plasma albumin concentrations has nor been shown to improve outcome in critical illness and in many of the traditional theraputic roles of albumin

* The recent fuss about albumin

The Cochrane report in the BMJ in July 1998 suggested that treatment with albumin was related to a 6% excess of deaths above control. Although this study was flawed in many ways, it has illustrated what many have believed for some time: that theraputic albumin therapy has little role in the management of most patients. Nevertheless, where albumin's use is well defined - in paediatrics / burns, it's abandonment does not appear justified at this time.

Why is albumin important?

1. Binding and transport.
2. Maintenance of colloid osmotic pressure.
3. Free radical scavenging.
4. Platelet function inhibition and antithrombotic effects.
5. Effects on vascular permeability.

Binding and transport
There are actually four binding sites on albumin and these have varying specificity for different substances.
Competitive binding of drugs may occur at the same sit or at different sites (conformational changes) [eg. warfarin and diazepam].
The drugs that are important for albumin binding are: warfarin, digoxin, NSAIDS, midazolam, thiopentone.
The relevence of a low albumin and drug binding is unknown.

Osmotic pressure
Albumin is responsible for 75 - 80 % of osmotic pressure.
Starling's equation: Transcapillary Flow = k [(Pcap + p i) - (Pi + p cap )]
Remember that albumin is the main protein both in the plasma and in the interstitium and it is the COP gradient rather than the absolute plasma value that is important: this is what distinguishes hypoalbuminaemia derived from redistribution (capillary leak) from that of pure full body deficiency.

Free Radicals
Albumin is a major source of sulphydryl groups, these "thiols" scavenge free radicals (nitrogen and oxygen species).
Albumin may be an important free radical scavenger in sepsis.

Anticoagulant effects
The anticoagulant and antithrombotic effects of albumin are poorly understood this may be due to binding nitric oxide radicals inhibiting inactivation and permitting a more prolonged antiaggregatory effect.
In diabetes, glycosylated albumin may increase the incidence of thrombotic events and atherosclerosis.

Capillary Membrane Permeability
In sepsis there is an increased rate of albumin loss into the tissues - this is probably related to increased capillary membrane permeability.

Source: 4um.com

What Is Albumin?

Albumin is an umbrella term for a type of protein which is water soluble. Numerous types of albumin can be found all over the natural world, and two of the most familiar examples of albumin can be found in egg whites and in human blood. Albumins are an important class of protein, and they are vitally important to health and well being for many organisms. Many plants and animals contain or secrete albumin.

A protein classified as albumin is globular, meaning that it is soluble in water. Globular proteins also have a roughly spherical structure. When combined with water, albumin and other globular proteins form a colloid, a solution which appears homogeneous although it actually contains multiple substances. The other type of protein, fibrous protein, such as that found in muscles, is not water soluble, and it has a different basic structure.

Source: wisegeek.com

Albumin 'Wiki'

Albumin (Latin: albus, white) refers generally to any protein that is water soluble, which is moderately soluble in concentrated salt solutions, and experiences heat coagulation (protein denaturation). Substances containing albumin, such as egg white, are called albuminoids.
A number of serum transport proteins are known to be evolutionarily related, including serum albumin, alpha-fetoprotein, vitamin D-blinding protein, and afamin.

Source: Wikipedia.