Hydrolysis of animal fat and vegetable oil with Mucor miehei esterase. Properties of the enzyme

Moskowitz, Gerard J.; Cassaigne, R; West, Isaac R.; Shen, T.; Feldman, Louis I.

doi:10.1021/jf60213a045

Cited by 40 publications

(7 citation statements)

References 13 publications

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“…16). Furthermore, RM lipase is known to react with different AG species faster than glycerol in (inter)esterification processes (17), and RM lipase selectively hydrolyzes tributyroylglycerol at acid pH (18). These facts lend further support to the postulated origin of non-C4-MAG species being C4-containing DAG.…”

Section: Resultsmentioning

confidence: 84%

Reaction selectivity of rhizomucor miehei lipase as influenced by monoacylation of sn‐glycerol

Parkin

2004

J Americ Oil Chem Soc

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Reaction selectivities were determined in multicompetitive reactions mediated by Rhizomucor miehei (RM) lipase at water activity of 0.19 in hexane. Saturated FA (C4-C18 even chain) and oleic acid (C18:1) were reacted with a single alcohol, glycerol, or α-or β-MAG containing C4, C10, C16, or C18:1 individually as alcohol cosubstrate. Similar patterns of broad FA selectivity toward C8-C18 FA were generally observed for esterification into specific acylglycerol (AG) pools with the different α/β-CX-MAG cosubstrates. Exceptions were enrichment of C18 in the MAG pool with α-C16-MAG substrate, and a general suppression of C4/C6 FA reactivity and a specific discrimination toward >C8 FA incorporation into the TAG pool, both for reactions with α-C10-and α-C16-MAG. RM lipase selectivity toward MAG was in descending order: β-Selectivity in channeling CX of the original CX-MAG substrates into higher AG species was in descending order:Aside from their characteristic FA selectivity, Burkholderia cepacia (PS-30) and RM lipases behaved similarly in terms of MAG selectivity as well as a general conservation of FA selectivity throughout the sequential steps of TAG assembly from FA and glycerol for processes designed to yield specifically structured TAG.The prospect of using lipases to prepare uniquely functional "structured glycerides" for food and allied industries represents an opportunity to add value to basal lipid resources (1). The scientific literature is rife with examples of empirical or archival accounts of how lipids may be transformed by lipases into derivatives of enhanced functionality for specific applications. However, to fully exploit the synthetic power of lipases for these purposes, a comprehensive understanding of substrate and product selectivity patterns is required. This would enable the development of cogent strategies to use specific lipases to convert various lipid mixtures into desired structured glyceride derivatives.One can envision the de novo assembly of structured TAG as a three-step, incremental process of selective acylation of each of the three sn-glycerol hydroxyl groups. Selectivity of enzymic reactions is quantitatively indexed in terms of specificity constants (k cat /K M , which is directly proportional to V max /K M ), and such constants are applicable at any substrate concentration (2). Therefore, quantifying enzyme selectivity in terms of kinetic constants allows one to predict enzyme behavior under conditions where different substrate profiles and concentrations may be considered or anticipated. Selectivity of several lipases toward a host of FA substrates has been quantified in terms of relative selectivity constants (often expressed in ratio format as relative α-values) by several research groups (3)(4)(5)(6)(7)(8)(9)(10)(11). In all cases, free alcohols or acetate esters of alcohol were employed as cosubstrates. What is not known is how progressive acylation of the snglycerol backbone, yielding different alcohol cosubstrates, may modulate lipase selectivity toward FA for subsequent est...

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Section: Resultsmentioning

confidence: 84%

Reaction selectivity of rhizomucor miehei lipase as influenced by monoacylation of sn‐glycerol

Parkin

2004

J Americ Oil Chem Soc

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“…In the food industry, carboxylate esters, lipophilic molecules that are released by the action of lipases, have been used as flavoring ingredients. In dairy products, both lipases and esterases are commonly used to produce desired flavors (Moskowitz et al 1977). Taste and flavor depend on the type of fatty acids chain released during the action of lipase.…”

Section: Introductionmentioning

confidence: 99%

Acceleration of Swiss cheese ripening by microbial lipase without affecting its quality characteristics

Rani

Jagtap

2018

J Food Sci Technol

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The effect of exogenous microbial lipase enzyme on the ripening of Swiss cheese (0, 200, and 800U lipase in 30 L milk) was investigated for the physicochemical, textural and sensory properties, along with its microstructure. The aim of this study was to investigate the application of microbial lipase to accelerate the ripening without affecting its original desirable quality characteristics. The effect of the microbial lipase was studied at different time periods (2, 30, 45, and 60 days) of the Swiss cheese ripening stages. Statistical analysis of the results showed that the physico-chemical parameters of cheese slightly increased during the ripening. Also, at all stages of the ripening hardness of Swiss cheese increased while the brittleness decreased. The number and size of the fat globules were also affected by the addition of the lipases. This study also showed that increase in the lipase amount had no significant change in quality and sensory parameters. Therefore, 200U of lipase was found to be sufficient to reduce the ripening time from 90 to 60 days by maintaining its genuine quality. Thus, this study suggested that the addition of microbial lipase may significantly reduce the cost of the cheese production by lowering the ripening period by 1 month and maintaining the quality of the final product.

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“…This slow rate of hydrolysis was also observed by Ibrahim and coworkers. 40,41 This could be explained by the structure of castor oil, in which ricinoleic acid was its main composition.…”

Section: Resultsmentioning

confidence: 99%

Comparative study of the hydrolysis of different oils by lipase‐immobilized membranes

Gupta

Ingole

Singh

et al. 2011

J of Applied Polymer Sci

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Hydrolysis of animal fat and vegetable oil with Mucor miehei esterase. Properties of the enzyme

Cited by 40 publications

References 13 publications

Reaction selectivity of rhizomucor miehei lipase as influenced by monoacylation of sn‐glycerol

Reaction selectivity of rhizomucor miehei lipase as influenced by monoacylation of sn‐glycerol

Acceleration of Swiss cheese ripening by microbial lipase without affecting its quality characteristics

Comparative study of the hydrolysis of different oils by lipase‐immobilized membranes

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