• Excellent Pectinesterase with High Quality
  • Excellent Pectinesterase with High Quality
  • Excellent Pectinesterase with High Quality
  • Excellent Pectinesterase with High Quality
  • Excellent Pectinesterase with High Quality
  • Excellent Pectinesterase with High Quality
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Excellent Pectinesterase with High Quality

CAS No.: 2944-68-5
Cor: Branco
Aparência: Em pó
Pacote de Transporte: Paper
Especificação: large
Marca Registrada: china

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Beijing, China
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Informação Básica.

N ° de Modelo.
E1422
Origem
China
Código HS
2930400000
Capacidade de Produção
5000kg/Year

Descrição de Produto

PE is synthesized by plants, molds, and bacteria. Only a few yeasts have been reported to produce it. It is not known to be synthesized by animals.

A. Plant Pectinesterase

PE is present in many plants and microorganisms (Versteeg, 1979). It was first identified in carrot by Fremy (1840), but this discovery was overlooked until 1925 when Kopaczewski (1925) reported its unique requirement of alkali salts. The isolates reported to date deesterify consecutive galacturonate monomers along the chain. More recent investigations were undertaken by Lineweaver and colleagues (Lineweaver and Ballou, 1943, 1945; Lineweaver and Jansen, 1951). Plant PE is inactivated below pH 7.

B. Microbial Pectinesterase

Microbial PE is an extracellular, inducible, or constitutive enzyme (depending on the origin). The substrate may be pectin, pectic acid, D-galacturonate or other carbohydrate material (Phaff, 1947; Bateman and Beer, 1965; Ogundero, 1988). The literature (for example, Perley and Page, 1971; Waggoner and Dimond, 1955; Starr and Nasuno, 1967; Ogundero, 1988) emphasizes specific enhancers, substrates, conditions, etc., for optimal production of PE by individual microorganisms.

C. Plant versus Microbial Pectinesterase

There are marked differences between microbial and plant PE. Fungal PE is generally more resistant to chemical agents and has an isoelectric point (pi) and pH optimum in the acidic range, in contrast to the alkaline pH range for plants. Microbial PE is more sensitive to heat and is less affected by salt (Lineweaver and Jansen, 1951; Kertesz, 1955). Some fungal PE catalyze reactions in a random manner. The properties of some microbial PE have been summarized by Fogarty and Kelly (1983).

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PE is synthesized by plants, molds, and bacteria. Only a few yeasts have been reported to produce it. It is not known to be synthesized by animals.

A. Plant Pectinesterase

PE is present in many plants and microorganisms (Versteeg, 1979). It was first identified in carrot by Fremy (1840), but this discovery was overlooked until 1925 when Kopaczewski (1925) reported its unique requirement of alkali salts. The isolates reported to date deesterify consecutive galacturonate monomers along the chain. More recent investigations were undertaken by Lineweaver and colleagues (Lineweaver and Ballou, 1943, 1945; Lineweaver and Jansen, 1951). Plant PE is inactivated below pH 7.

B. Microbial Pectinesterase

Microbial PE is an extracellular, inducible, or constitutive enzyme (depending on the origin). The substrate may be pectin, pectic acid, D-galacturonate or other carbohydrate material (Phaff, 1947; Bateman and Beer, 1965; Ogundero, 1988). The literature (for example, Perley and Page, 1971; Waggoner and Dimond, 1955; Starr and Nasuno, 1967; Ogundero, 1988) emphasizes specific enhancers, substrates, conditions, etc., for optimal production of PE by individual microorganisms.

C. Plant versus Microbial Pectinesterase

There are marked differences between microbial and plant PE. Fungal PE is generally more resistant to chemical agents and has an isoelectric point (pi) and pH optimum in the acidic range, in contrast to the alkaline pH range for plants. Microbial PE is more sensitive to heat and is less affected by salt (Lineweaver and Jansen, 1951; Kertesz, 1955). Some fungal PE catalyze reactions in a random manner. The properties of some microbial PE have been summarized by Fogarty and Kelly (1983).

Excellent Pectinesterase with High QualityExcellent Pectinesterase with High QualityExcellent Pectinesterase with High QualityExcellent Pectinesterase with High QualityExcellent Pectinesterase with High QualityExcellent Pectinesterase with High Quality
 

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