2007
DOI: 10.1007/s12010-007-8073-3
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Immobilization of Yarrowia lipolytica Lipase—a Comparison of Stability of Physical Adsorption and Covalent Attachment Techniques

Abstract: Lipase immobilization offers unique advantages in terms of better process control, enhanced stability, predictable decay rates and improved economics. This work evaluated the immobilization of a highly active Yarrowia lipolytica lipase (YLL) by physical adsorption and covalent attachment. The enzyme was adsorbed on octyl-agarose and octadecyl-sepabeads supports by hydrophobic adsorption at low ionic strength and on MANAE-agarose support by ionic adsorption. CNBr-agarose was used as support for the covalent att… Show more

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Cited by 45 publications
(22 citation statements)
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“…The first methodology to be tested was the physical adsorption on highly hydrophobic supports with different characteristics such as octyl-agarose, PHB, and amberlite XAD-4 (Table 1) to take advantage of the complex mechanism of lipases as a tool that allows the immobilization via hydrophobic interaction at very low ionic strength [9, 20, 21]. Lipases recognize these surfaces similarly to those of their natural substrates (drops of oil), yielding immobilized derivative with open and hyperactivated structures [9, 21].…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The first methodology to be tested was the physical adsorption on highly hydrophobic supports with different characteristics such as octyl-agarose, PHB, and amberlite XAD-4 (Table 1) to take advantage of the complex mechanism of lipases as a tool that allows the immobilization via hydrophobic interaction at very low ionic strength [9, 20, 21]. Lipases recognize these surfaces similarly to those of their natural substrates (drops of oil), yielding immobilized derivative with open and hyperactivated structures [9, 21].…”
Section: Resultsmentioning
confidence: 99%
“…These enzymes are strongly adsorbed onto hydrophobic interfaces through the lid that covers their active site, recognizing these supports as their natural substrate (hydrophobic oil interfaces). This technique is easy, cheap, and allows facile recycling of the support at the end of the life of the enzyme [9, 2022]. Enzymes can be also reversibly immobilized on ionic exchange supports.…”
Section: Introductionmentioning
confidence: 99%
“…Instead, lipase enzymes could be applied for biodiesel production in an eco-friendly manner [9,11]. For decades, much of the literature relevant to this topic has been focused largely on the process of biodiesel production using microbial lipases [9,12]. 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.…”
Section: Introductionmentioning
confidence: 99%
“…Many diverse immobilization methods have been developed for this purpose. Among them are some methods which require rigid supports: most notably, hydrophobic adsorption [12], ionic immobilization [15,16], and covalent immobilization [17][18][19]. Choosing the most suitable immobilization method has become an important factor for transesterification efficiency of microbial lipases.…”
Section: Introductionmentioning
confidence: 99%
“…The treatment of adsorbed enzyme on support with cross-linker can solve the above problems to a certain extent [9][10][11][12][13]. Glutaraldehyde is the most effective cross-linker [14][15][16], which can enhance the interactions between enzyme and support.…”
Section: Introductionmentioning
confidence: 99%