Enzymes in Meat Processing

Lantto, Raija; Kruus, Kristiina; Puolanne, Eero; Honkapää, Kaisu; Roininen, Katariina; Büchert, Johanna

doi:10.1002/9781444309935.ch12

Cited by 9 publications

(5 citation statements)

References 149 publications

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“…The meat-tenderization process is mainly enzymatic, and it involves the utilization of microbial or plant enzymes [5]. The tenderization of meat with proteolytic enzymes is becoming a popular method, and, recently, proteolytic enzymes derived from the ginger rhizome (Zingiber officinale Roscoe) were introduced as effective enzymes for tenderizing the tough meat that arises from old animals [6].…”

Section: Introductionmentioning

confidence: 99%

Structural Changes, Electrophoretic Pattern, and Quality Attributes of Camel Meat Treated with Fresh Ginger Extract and Papain Powder

Abdel-Naeem

Talaat

Imre

et al. 2022

Foods

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Camel is a valuable source of meat for African and Asian countries; however, the most important problem associated with camel meat is its extreme toughness. This toughness has been attributed to its contents of connective tissue, which become more crossly linked in old animals. The toughness of camel meat decreases the consumer acceptance of this meat and reduces its chances of being utilized as a raw material for further processing into meat products. Ginger and papain were used in the current study as tenderizing enzymes, and the structural changes, electrophoretic pattern, physicochemical characteristics, and sensory scores of the treated meat were examined. The treatment of camel meat with ginger and papain resulted in marked destructive changes in the connective tissue and myofibers, and a reduction in the protein bands, with a consequent improvement in its tenderness. All the enzyme-treated samples exhibited significant increases in the protein solubility, with significant decreases in the shear-force values. Moreover, an improvement in the sensory scores of the raw and cooked meat and a reduction in the bacterial counts after the treatments were recorded. Ginger and papain induced a significant improvement in the physicochemical characteristics, sensory attributes, and bacterial counts of the camel meat; therefore, these materials can be utilized by meat processors to boost the consumer acceptance of this meat, and to increase its suitability as a raw material for further meat processing.

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Section: Introductionmentioning

confidence: 99%

Structural Changes, Electrophoretic Pattern, and Quality Attributes of Camel Meat Treated with Fresh Ginger Extract and Papain Powder

Abdel-Naeem

Talaat

Imre

et al. 2022

Foods

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“…The ability of tyrosinases to generate o-quinones on proteins is well documented, at least at high substrate concentrations. Tyrosinases and phenol oxidases have been known for decades to mediate cross-linking between proteins in meat, 37 whey, 38 and flour 39 via nonselective tyrosine-tyrosine, tyrosine-cysteine, and tyrosine-lysine linkages. More recently, Long and Hedstrom described abTYR-mediated oxidation of multiple tyrosine residues in a hemagglutinin tag (YPYDVPDYA) and similar variants at the C-terminus of E. coli dihydrofolate reductase.…”

Section: ■ Introductionmentioning

confidence: 99%

Tyrosinase-Mediated Oxidative Coupling of Tyrosine Tags on Peptides and Proteins

et al. 2020

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Oxidative coupling (OC) through o-quinone intermediates has been established as an efficient and site-selective way to modify protein N-termini and the unnatural amino acid p-aminophenylalanine (paF). Recently, we reported that the tyrosinase-mediated oxidation of phenol-tagged cargo molecules is a particularly convenient method of generating o-quinones in situ. The coupling partners can be easily prepared and stored, the reaction takes place under mild conditions (phosphate buffer, pH 6.5, 4 to 23 °C), and dissolved oxygen is the only oxidant required. Here, we show an important extension of this chemistry for the activation of tyrosine residues that project into solution from the N or C-termini of peptide and protein substrates. Generating the o-quinone electrophiles from tyrosine allows greater flexibility in choosing the nucleophilic coupling partner and expands the scope of the reaction to include C-terminal positions. We also introduce a new bacterial tyrosinase enzyme that shows improved activation for some tyrosine substrates. The efficacy of several secondary amines and aniline derivatives was evaluated in the coupling reactions, providing important information for coupling partner design. This strategy was used to modify the C-termini of an antibody scFv construct and of Protein L, a human IgG kappa light chain binding protein. The use of the modified proteins as immunolabeling agents was also demonstrated.

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“…The process reduces the viscosity by cleaving peptide bonds to release free amino acids and low molecular weight ( Mw ) peptides (Villamil et al ., ). It also enhances flavour potential by generating meat flavour precursors and exposing sulfhydryl group (Lantto et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Effects of enzymatic hydrolysis treatments on the physicochemical properties of beef bone extract using endo‐ and exoproteases

Chiang

Loveday

Hardacre

et al. 2018

Int J of Food Sci Tech

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This study reported the effects of enzymatic hydrolysis treatments on the physiochemical properties of beef bone extract using endo-and exoproteases. Each enzyme hydrolysis kinetics were studied using Michaelis-Menten model, and the ideal E/S ratio obtained for Protamex Ò (P), bromelain (B) and Flavourzyme Ò (F) was found to be 1.10%, 1.60% and 4.70% w/w, respectively. Seven hydrolysates were produced from single (P, B, F), simultaneous (P + F, B + F) and sequential (P > F, B > F) treatments, where bone extract hydrolysed by Flavourzyme Ò exhibited highest DH and proportion of low molecular weight (Mw) peptides (<5000 Da) in single treatment. When Flavourzyme Ò was used with Protamex Ò or bromelain in simultaneous or sequential treatments, no significant differences in Mw distribution, exposed SH content, SS content and viscosity were evident compared with Flavourzyme Ò only. This indicated that without the addition of other enzymes, Flavourzyme Ò was capable of increasing the proportion of low Mw peptides and reduce viscosity.

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Enzymes in Meat Processing

Cited by 9 publications

References 149 publications

Structural Changes, Electrophoretic Pattern, and Quality Attributes of Camel Meat Treated with Fresh Ginger Extract and Papain Powder

Structural Changes, Electrophoretic Pattern, and Quality Attributes of Camel Meat Treated with Fresh Ginger Extract and Papain Powder

Tyrosinase-Mediated Oxidative Coupling of Tyrosine Tags on Peptides and Proteins

Effects of enzymatic hydrolysis treatments on the physicochemical properties of beef bone extract using endo‐ and exoproteases

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