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Potential and utilization of thermophiles and thermostable enzymes in biorefining.

Turner P, Mamo G, Karlsson EN - Microb. Cell Fact. (2007)

Bottom Line: Many of these processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lowered risk of contamination.Strategies that enhance thermostablity of enzymes both in vivo and in vitro are also assessed.Moreover, this review deals with efforts made on developing vectors for expressing recombinant enzymes in thermophilic hosts.

View Article: PubMed Central - HTML - PubMed

Affiliation: Dept Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, PO Box 124, SE-221 00 Lund, Sweden. pernilla.turner@biotek.lu.se

ABSTRACT
In today's world, there is an increasing trend towards the use of renewable, cheap and readily available biomass in the production of a wide variety of fine and bulk chemicals in different biorefineries. Biorefineries utilize the activities of microbial cells and their enzymes to convert biomass into target products. Many of these processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lowered risk of contamination. Thermophiles have often been proposed as sources of industrially relevant thermostable enzymes. Here we discuss existing and potential applications of thermophiles and thermostable enzymes with focus on conversion of carbohydrate containing raw materials. Their importance in biorefineries is explained using examples of lignocellulose and starch conversions to desired products. Strategies that enhance thermostablity of enzymes both in vivo and in vitro are also assessed. Moreover, this review deals with efforts made on developing vectors for expressing recombinant enzymes in thermophilic hosts.

No MeSH data available.


Enzymatic attack on part of an amylopectin molecule. Glucose molecules are indicated as circles and the reducing ends are marked by a line through the circle.
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Figure 2: Enzymatic attack on part of an amylopectin molecule. Glucose molecules are indicated as circles and the reducing ends are marked by a line through the circle.

Mentions: Starch from cultivated plants is one of the most abundant and accessible energy sources in the world. It consists of amylose and amylopectin, and an overview of the principal structure indicating sites of enzymatic attack is given in Fig. 2. Corn is the most used crop in starch processing in industries, but wheat, potato and tapioca are also important crops while rice, sorghum, sweet potato, arrowroot, sago and mung beans are used to a lesser extent [75].


Potential and utilization of thermophiles and thermostable enzymes in biorefining.

Turner P, Mamo G, Karlsson EN - Microb. Cell Fact. (2007)

Enzymatic attack on part of an amylopectin molecule. Glucose molecules are indicated as circles and the reducing ends are marked by a line through the circle.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC1851020&req=5

Figure 2: Enzymatic attack on part of an amylopectin molecule. Glucose molecules are indicated as circles and the reducing ends are marked by a line through the circle.
Mentions: Starch from cultivated plants is one of the most abundant and accessible energy sources in the world. It consists of amylose and amylopectin, and an overview of the principal structure indicating sites of enzymatic attack is given in Fig. 2. Corn is the most used crop in starch processing in industries, but wheat, potato and tapioca are also important crops while rice, sorghum, sweet potato, arrowroot, sago and mung beans are used to a lesser extent [75].

Bottom Line: Many of these processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lowered risk of contamination.Strategies that enhance thermostablity of enzymes both in vivo and in vitro are also assessed.Moreover, this review deals with efforts made on developing vectors for expressing recombinant enzymes in thermophilic hosts.

View Article: PubMed Central - HTML - PubMed

Affiliation: Dept Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, PO Box 124, SE-221 00 Lund, Sweden. pernilla.turner@biotek.lu.se

ABSTRACT
In today's world, there is an increasing trend towards the use of renewable, cheap and readily available biomass in the production of a wide variety of fine and bulk chemicals in different biorefineries. Biorefineries utilize the activities of microbial cells and their enzymes to convert biomass into target products. Many of these processes require enzymes which are operationally stable at high temperature thus allowing e.g. easy mixing, better substrate solubility, high mass transfer rate, and lowered risk of contamination. Thermophiles have often been proposed as sources of industrially relevant thermostable enzymes. Here we discuss existing and potential applications of thermophiles and thermostable enzymes with focus on conversion of carbohydrate containing raw materials. Their importance in biorefineries is explained using examples of lignocellulose and starch conversions to desired products. Strategies that enhance thermostablity of enzymes both in vivo and in vitro are also assessed. Moreover, this review deals with efforts made on developing vectors for expressing recombinant enzymes in thermophilic hosts.

No MeSH data available.