Biotechnology for Fuels and Chemicals 2007
DOI: 10.1007/978-1-60327-526-2_19
|View full text |Cite
|
Sign up to set email alerts
|

Immobilization of Yarrowia lipolytica Lipase—A Comparison of Stability of Physical Adsorption and Covalent Attachment Techniques

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
7
0

Year Published

2011
2011
2021
2021

Publication Types

Select...
5
1

Relationship

0
6

Authors

Journals

citations
Cited by 7 publications
(7 citation statements)
references
References 25 publications
0
7
0
Order By: Relevance
“…On this last point, benefits of enzyme immobilization include: facilitating the separation of products from the active enzymes; and increasing enzyme shelf life by protecting them against proteolysis, thermal and chemical denaturation. [42][43][44] There are several methods for the industrial immobilization of enzymes, such as: covalent linkage 44 or adsorption 45 (generally ionic) to a support; entrapment within a matrix; 46 and direct enzyme crosslinking. 47 There are disadvantages of these current methods, however, which include: the leakage of the protein from supports; loss of enzyme activity due to protein unfolding or misfolding; and restricted protein mobility and/or access of substrates due to inappropriate cross-linking.…”
Section: Resultsmentioning
confidence: 99%
“…On this last point, benefits of enzyme immobilization include: facilitating the separation of products from the active enzymes; and increasing enzyme shelf life by protecting them against proteolysis, thermal and chemical denaturation. [42][43][44] There are several methods for the industrial immobilization of enzymes, such as: covalent linkage 44 or adsorption 45 (generally ionic) to a support; entrapment within a matrix; 46 and direct enzyme crosslinking. 47 There are disadvantages of these current methods, however, which include: the leakage of the protein from supports; loss of enzyme activity due to protein unfolding or misfolding; and restricted protein mobility and/or access of substrates due to inappropriate cross-linking.…”
Section: Resultsmentioning
confidence: 99%
“…These results indicated that relatively weaker hydrophobic environment did not contribute to the improvement of specific activity of immobilized lipase. The advantages of PGMA were mainly due to the covalent attachment between lipase and the microspheres [22,28,36]. Catalytic efficiency, reusability, and stability of immobilized lipase…”
Section: Influence Of Different Hydrophobicity Degree On Lipase Immobmentioning
confidence: 99%
“…Therefore, many researchers focused on covalent binding of lipase molecules with the functional groups of carriers to obtain stable enzyme performance [21][22][23]. The functional groups of carriers mainly include epoxy [24,25], amide [26], and aldehyde group [27].…”
Section: Introductionmentioning
confidence: 99%
“…Many diverse immobilization methods have been developed for this purpose. Among these are some methods that require rigid supports: most notably, covalent immobilization [9,11,17], ionic immobilization [20], and hydrophobic adsorption [2]. However, methods for the immobilization of enzymes without the use of supports are gaining in importance because they offer the advantages of high volumetric productivity and lower production costs [16,17].…”
mentioning
confidence: 99%
“…Here, lipase enzymes could be applied for biodiesel production in an eco-friendly manner [14]. For decades, much of the literature relevant to this topic has been focused largely on the process of biodiesel production using microbial lipases [2,9,11,20]. Among these, Candida antarctica lipase B (CalB) has been most frequently utilized, owing primarily to its profound ability to carry out the biodiesel production reaction with a variety of plant oils.…”
mentioning
confidence: 99%